==== Reference: Usmani SS, Bedi G, Samuel JS, Singh S, Kalra S, Kumar P, et al. (2017) THPdb: Database of FDA-approved peptide and protein therapeutics. PLoS ONE 12(7) e0181748.====

Detailed description page of THPdb


Details of Th1042 which contains 17 entries.


Entry 1
(1) Primary information
ID1288
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetCollagen 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 NameCordase
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful Linkhttp://www.lantus.com/considering/lantus-solostar-features/lantus-solostar-pen
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 2
(2) Primary information
ID1289
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionGrafco Silver Nitrate (silver nitrate topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameSantyl
CompanyAdvance Biofactures Corp
Brand DiscriptionCollagenase 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 forUsed to remove dead skin from wounds and burned areas. Santyl ointment is an enzymatic debriding ointment which works by breaking down dead skin.
Chemical NameN.A.
FormulationCollagenase 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 37°C for 24 hours. The nu
Physcial AppearanceSterile enzymatic debriding ointment
Route of AdministrationApply on the affected area.
Recommended DosageCollagenase Santyl Ointment should be applied once daily (or more frequently if the dressing becomes soiled as from incontinence).
ContraindicationHypersensitivity
Side EffectsRash; 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 Linkhttp://www.santyl.com
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 3
(3) Primary information
ID1290
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionSilvrSTAT (silver topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful Linkhttp://www.rxlist.com/santyl-drug.htm
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 4
(4) Primary information
ID1291
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionThermazene (silver sulfadiazine topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful Linkhttp://www.drugs.com/cdi/santyl-ointment.html
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 5
(5) Primary information
ID1292
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug Interactionsilver / zinc oxide topical
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 6
(6) Primary information
ID1293
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionSilvaSorb (silver topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 7
(7) Primary information
ID1294
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionMersol (thimerosal topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 8
(8) Primary information
ID1295
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug Interactionsilver sulfadiazine topical
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 9
(9) Primary information
ID1296
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionSSD AF (silver sulfadiazine topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 10
(10) Primary information
ID1297
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionSilvadene Cream 1% (silver sulfadiazine topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 11
(11) Primary information
ID1298
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionSilvadene (silver sulfadiazine topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 12
(12) Primary information
ID1299
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionSSD (silver sulfadiazine topical)
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 13
(13) Primary information
ID1300
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug Interactionsilver nitrate topical
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 14
(14) Primary information
ID1301
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug Interactionthimerosal topical
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful LinkN.A.
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 15
(15) Primary information
ID1302
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameXiaflex
CompanyAuxilium
Brand DiscriptionIt 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 forXIAFLEX 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 NameN.A.
FormulationXIAFLEX 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 AppearanceSterile lyophilized powder (white cake) and must be reconstituted with the provided diluent prior to use.
Route of AdministrationIntralesional Injection
Recommended DosageThe 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
ContraindicationThe treatment of Peyronie's plaques that involve the penile urethra due to potential risk to this structure.
Side EffectsSwelling, 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 Linkhttps://www.xiaflex.com
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 16
(16) Primary information
ID1303
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationPatients with a history of hypersensitivity to XIAFLEX or to collagenase used in any other therapeutic application or application method
Side EffectsN.A.
Useful Linkhttp://www.drugs.com/xiaflex.html
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)


Entry 17
(17) Primary information
ID1304
ThPP IDTh1042
Therapeutic Peptide/Protein NameCollagenase
SequenceMKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta
Functional ClassificationIc
Molecular Weight112023.2
Chemical FormulaC5028H7666N1300O1564S21
Isoelectric Point5.58
Hydrophobicity-0.714
Melting Point (℃)N.A.
Half LifeN.A.
DescriptionThis enzyme is derived from fermentation of Clostridium histolyticum
Indication/DiseaseIt promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers.
PharmacodynamicsHelps 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 ActionCollagenase 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.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
ClearanceN.A.
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful Linkhttp://www.rxlist.com/xiaflex-drug.htm
PubMed ID11937475
3-D StructureTh1042 (View) or (Download)