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Th1042 details

Primary information
ID 1288
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction N.A.
Target Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain,Collagen alpha-2(I) chain
Information of corresponding available drug in the market
Brand Name Cordase
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link http://www.lantus.com/considering/lantus-solostar-features/lantus-solostar-pen
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1289
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Grafco Silver Nitrate (silver nitrate topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name Santyl
Company Advance Biofactures Corp
Brand Discription Collagenase Santyl ointment is a sterile enzymatic debriding ointment which contains 250 collagenase units per gram of white petrolatum USP. The enzyme collagenase is derived from the fermentation by Clostridium histolyticum. It possesses the unique abili
Prescribed for Used to remove dead skin from wounds and burned areas. Santyl ointment is an enzymatic debriding ointment which works by breaking down dead skin.
Chemical Name N.A.
Formulation Collagenase Santyl Ointment contains 250 units of collagenase enzyme per gram of white petrolatum USP. The potency assay of collagenase is based on the digestion of undenatured collagen (from bovine Achilles tendon) at pH 7.2 and 37Â°C for 24 hours. The nu
Physcial Appearance Sterile enzymatic debriding ointment
Route of Administration Apply on the affected area.
Recommended Dosage Collagenase Santyl Ointment should be applied once daily (or more frequently if the dressing becomes soiled as from incontinence).
Contraindication Hypersensitivity
Side Effects Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; signs of infection (eg, fever, chills, or persistent sore throat).
Useful Link http://www.santyl.com
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1290
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction SilvrSTAT (silver topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link http://www.rxlist.com/santyl-drug.htm
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1291
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Thermazene (silver sulfadiazine topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link http://www.drugs.com/cdi/santyl-ointment.html
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1292
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction silver / zinc oxide topical
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1293
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction SilvaSorb (silver topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1294
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Mersol (thimerosal topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1295
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction silver sulfadiazine topical
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1296
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction SSD AF (silver sulfadiazine topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1297
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Silvadene Cream 1% (silver sulfadiazine topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1298
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Silvadene (silver sulfadiazine topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1299
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction SSD (silver sulfadiazine topical)
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1300
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction silver nitrate topical
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1301
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction thimerosal topical
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link N.A.
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1302
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction N.A.
Target N.A.
Information of corresponding available drug in the market
Brand Name Xiaflex
Company Auxilium
Brand Discription It contains purified collagenase clostridium histolyticum, consisting of two microbial collagenases in a defined mass ratio, Collagenase AUX-I and Collagenase AUX-II, which are isolated and purified from the fermentation of Clostridium histolyticum bacter
Prescribed for XIAFLEX is indicated for the treatment of adult patients with Dupuytren's contracture with a palpable cord. XIAFLEX is also indicated for the treatment of adult men with Peyronie's disease with a palpable plaque and curvature deformity of at least 30 degr
Chemical Name N.A.
Formulation XIAFLEX is available in single-use, glass vials containing 0.9 mg of collagenase clostridium histolyticum. Each vial also contains 0.5 mg of hydrochloric acid, 18.5 mg of sucrose, and 1.1 mg of tromethamine.
Physcial Appearance Sterile lyophilized powder (white cake) and must be reconstituted with the provided diluent prior to use.
Route of Administration Intralesional Injection
Recommended Dosage The dose of XIAFLEX is 0.58 mg per injection into a palpable cord with a contracture of a metacarpophalangeal (MP) joint or a proximal interphalangeal (PIP) joint
Contraindication The treatment of Peyronie's plaques that involve the penile urethra due to potential risk to this structure.
Side Effects Swelling, bruising, or bleeding where the medicine was injected; mild pain or tenderness in the treated hand; swollen glands in your elbow or underarm; itching, redness, or warmth of the skin; cracked skin; or underarm pain.
Useful Link https://www.xiaflex.com
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1303
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction N.A.
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication Patients with a history of hypersensitivity to XIAFLEX or to collagenase used in any other therapeutic application or application method
Side Effects N.A.
Useful Link http://www.drugs.com/xiaflex.html
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

Primary information
ID 1304
ThPP ID Th1042
Therapeutic Peptide/Protein Name Collagenase
Sequence MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification Ic
Molecular Weight 112023.2
Chemical Formula C5028H7666N1300O1564S21
Isoelectric Point 5.58
Hydrophobicity -0.714
Melting Point (℃) N.A.
Half Life N.A.
Description This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution N.A.
Clearance N.A.
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction N.A.
Target N.A.
Information of corresponding available drug in the market
Brand Name N.A.
Company N.A.
Brand Discription N.A.
Prescribed for N.A.
Chemical Name N.A.
Formulation N.A.
Physcial Appearance N.A.
Route of Administration N.A.
Recommended Dosage N.A.
Contraindication N.A.
Side Effects N.A.
Useful Link http://www.rxlist.com/xiaflex-drug.htm
PubMed ID 11937475
3-D Structure Th1042 (View) or (Download)

OSDDlinux

Raghava's Group

IMTECH

CSIR

CRDD
CPPSITE 2.0

Primary information
ID	1288
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	N.A.
Target	Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain,Collagen alpha-2(I) chain
Information of corresponding available drug in the market
Brand Name	Cordase
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	http://www.lantus.com/considering/lantus-solostar-features/lantus-solostar-pen
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1289
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Grafco Silver Nitrate (silver nitrate topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	Santyl
Company	Advance Biofactures Corp
Brand Discription	Collagenase Santyl ointment is a sterile enzymatic debriding ointment which contains 250 collagenase units per gram of white petrolatum USP. The enzyme collagenase is derived from the fermentation by Clostridium histolyticum. It possesses the unique abili
Prescribed for	Used to remove dead skin from wounds and burned areas. Santyl ointment is an enzymatic debriding ointment which works by breaking down dead skin.
Chemical Name	N.A.
Formulation	Collagenase Santyl Ointment contains 250 units of collagenase enzyme per gram of white petrolatum USP. The potency assay of collagenase is based on the digestion of undenatured collagen (from bovine Achilles tendon) at pH 7.2 and 37Â°C for 24 hours. The nu
Physcial Appearance	Sterile enzymatic debriding ointment
Route of Administration	Apply on the affected area.
Recommended Dosage	Collagenase Santyl Ointment should be applied once daily (or more frequently if the dressing becomes soiled as from incontinence).
Contraindication	Hypersensitivity
Side Effects	Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; signs of infection (eg, fever, chills, or persistent sore throat).
Useful Link	http://www.santyl.com
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1290
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	SilvrSTAT (silver topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	http://www.rxlist.com/santyl-drug.htm
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1291
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Thermazene (silver sulfadiazine topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	http://www.drugs.com/cdi/santyl-ointment.html
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1292
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	silver / zinc oxide topical
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1293
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	SilvaSorb (silver topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1294
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Mersol (thimerosal topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1295
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	silver sulfadiazine topical
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1296
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	SSD AF (silver sulfadiazine topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1297
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Silvadene Cream 1% (silver sulfadiazine topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1298
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Silvadene (silver sulfadiazine topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1299
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	SSD (silver sulfadiazine topical)
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1300
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	silver nitrate topical
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1301
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	thimerosal topical
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	N.A.
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1302
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	N.A.
Target	N.A.
Information of corresponding available drug in the market
Brand Name	Xiaflex
Company	Auxilium
Brand Discription	It contains purified collagenase clostridium histolyticum, consisting of two microbial collagenases in a defined mass ratio, Collagenase AUX-I and Collagenase AUX-II, which are isolated and purified from the fermentation of Clostridium histolyticum bacter
Prescribed for	XIAFLEX is indicated for the treatment of adult patients with Dupuytren's contracture with a palpable cord. XIAFLEX is also indicated for the treatment of adult men with Peyronie's disease with a palpable plaque and curvature deformity of at least 30 degr
Chemical Name	N.A.
Formulation	XIAFLEX is available in single-use, glass vials containing 0.9 mg of collagenase clostridium histolyticum. Each vial also contains 0.5 mg of hydrochloric acid, 18.5 mg of sucrose, and 1.1 mg of tromethamine.
Physcial Appearance	Sterile lyophilized powder (white cake) and must be reconstituted with the provided diluent prior to use.
Route of Administration	Intralesional Injection
Recommended Dosage	The dose of XIAFLEX is 0.58 mg per injection into a palpable cord with a contracture of a metacarpophalangeal (MP) joint or a proximal interphalangeal (PIP) joint
Contraindication	The treatment of Peyronie's plaques that involve the penile urethra due to potential risk to this structure.
Side Effects	Swelling, bruising, or bleeding where the medicine was injected; mild pain or tenderness in the treated hand; swollen glands in your elbow or underarm; itching, redness, or warmth of the skin; cracked skin; or underarm pain.
Useful Link	https://www.xiaflex.com
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1303
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	N.A.
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	Patients with a history of hypersensitivity to XIAFLEX or to collagenase used in any other therapeutic application or application method
Side Effects	N.A.
Useful Link	http://www.drugs.com/xiaflex.html
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)

Primary information
ID	1304
ThPP ID	Th1042
Therapeutic Peptide/Protein Name	Collagenase
Sequence	MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional Classification	Ic
Molecular Weight	112023.2
Chemical Formula	C5028H7666N1300O1564S21
Isoelectric Point	5.58
Hydrophobicity	-0.714
Melting Point (℃)	N.A.
Half Life	N.A.
Description	This enzyme is derived from fermentation of Clostridium histolyticum
Indication/Disease	It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
Pharmacodynamics	Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.
Mechanism of Action	Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	N.A.
Clearance	N.A.
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	N.A.
Target	N.A.
Information of corresponding available drug in the market
Brand Name	N.A.
Company	N.A.
Brand Discription	N.A.
Prescribed for	N.A.
Chemical Name	N.A.
Formulation	N.A.
Physcial Appearance	N.A.
Route of Administration	N.A.
Recommended Dosage	N.A.
Contraindication	N.A.
Side Effects	N.A.
Useful Link	http://www.rxlist.com/xiaflex-drug.htm
PubMed ID	11937475
3-D Structure	Th1042 (View) or (Download)