3.4.24.42: atrolysin C
This is an abbreviated version!
For detailed information about atrolysin C, go to the full flat file.
Word Map on EC 3.4.24.42
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3.4.24.42
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cartilage
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articular
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osteoarthritis
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joint
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chondrocytes
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proteoglycans
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explants
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metalloproteinases
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collagen
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adamts-4
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glycosaminoglycans
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thrombospondin
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synovial
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disintegrin
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knee
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neoepitope
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interglobular
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arthritic
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mmp-1
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aggrecanolysis
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chondroitin
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aggrecan-degrading
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timp-3
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nitege
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versican
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disintegrin-like
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interleukin-1alpha
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chondroprotective
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igd
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matrix-degrading
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adamalysin
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subchondral
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meniscal
- 3.4.24.42
- cartilage
-
articular
- osteoarthritis
- joint
- chondrocytes
- proteoglycans
-
explants
- metalloproteinases
- collagen
- adamts-4
- glycosaminoglycans
- thrombospondin
- synovial
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disintegrin
- knee
-
neoepitope
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interglobular
-
arthritic
- mmp-1
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aggrecanolysis
- chondroitin
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aggrecan-degrading
- timp-3
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nitege
- versican
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disintegrin-like
- interleukin-1alpha
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chondroprotective
- igd
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matrix-degrading
- adamalysin
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subchondral
-
meniscal
Reaction
Cleavage of His5-/-Leu, His10-/-Leu, Ala14-/-Leu, Tyr16-/-Leu and Gly23-/-Phe bonds in B chain of insulin. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1 =
Synonyms
aggrecanase, atrolysin, Crotalus atrox metalloendopeptidase c, hemorrhagic metalloproteinase HT-d, Hemorrhagic toxin c and d, PI metalloproteinase, Ruberlysin
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.42 - atrolysin C
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REACTION DIAGRAM
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
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Acetyl-Val-Ala-Leu-Leu-Ala + H2O
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best substrate of synthetic acetylated pentapeptides
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angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His + Pro + Phe-His-Leu
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleaved at His-Pro and Pro-Phe
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Gelatin of collagen type V + H2O
Hydrolyzed gelatin of collagen type V
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i.e. denatured collagen, hydrolysis at 38øC and above, not below
MW 130000, MW 118000, MW 93000 and MW 85000 fragments
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Luteinizing hormone-releasing hormone + H2O
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cleavage sites: Trp3-Ser4, Gly6-Leu7
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Met-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
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i.e. Tyr-Gly-Gly-Phe-Met, cleavage site: Gly3-Phe4
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Basement membrane preparation + H2O
Soluble peptides
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poor substrate: component band a
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involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
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Basement membranes surrounding capillaries + H2O
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together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
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Basement membranes surrounding capillaries + H2O
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together with atrolysins B and E member of the class P-I hemorrhagic toxins
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Basement membranes surrounding capillaries + H2O
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less potent hemorrhagic toxins of Crotalus atrox venom
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bovine aggrecan monomer + H2O
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purified atrolysin C can cleave at the cleavage sites VIPEN + FFBVG and ITEGE + ARGSV independently
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Hydrolyzed collagen type IV
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basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
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Collagen type IV + H2O
Hydrolyzed collagen type IV
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basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
MW 170000, MW 164000, MW 125000, MW 110000, MW 940000 and MW 64000 fragments
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Hydrolyzed gelatin of collagen type I
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i.e. denatured collagen
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Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
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i.e. denatured collagen
MW 60000 and MW 50000 fragments
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Leu-Val-Glu-Ala + Leu-Tyr-Leu
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cleavage at Ala-Leu
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Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
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peptide derived from insulin B-chain, best substrate
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Oxidized insulin B-chain + H2O
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cleavage at His5-Leu6, His10-Leu11, Ala14-Leu15 (most rapidly cleaved bond)
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Oxidized insulin B-chain + H2O
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cleaves the same bonds as atrolysin B and A (the latter except Gly23-Phe24)
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Oxidized insulin B-chain + H2O
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cleavage at Tyr16-Leu17 (slightly less rapidly cleaved bond)
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Oxidized insulin B-chain + H2O
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Crotalus ruber ruber toxin HT-3 does not cleave the His5-Leu6 bond which is cleaved by HT-2
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VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
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von Willebrand factor + H2O
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i.e. VWF, is a large, multidomain glycoprotein, atrolysin C does not require specific interaction with the VWA1 domain and likely cleaves VWF in a nonlocalized manner, cleavage in sequences MSMG-/-VSG, MSMG(C)V-/-G, LVPDS-/-H, and MSMG(C)VSG, after the D domain and the cystine knot-like domain, atrolysin C cleaves VWF at widely distributed sites identified next to VWD3 and VWD4 domains, overview
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additional information
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no hydrolysis of interstitial collagen, native type I collagen
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additional information
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cleavage specificity, compared to hemorrhagic toxins a and b
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additional information
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substrate requirements: small aliphatic residues at P1 (Ala or Gly) and Leu at P2
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additional information
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substrate digestion patterns differ from those of atrolysins A and E
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additional information
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peptides of four residues or less are not hydrolyzed, no significant degradation of fibrin
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