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Information on EC 3.4.24.42 - atrolysin C for references in articles please use BRENDA:EC3.4.24.42Word Map on EC 3.4.24.42
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The expected taxonomic range for this enzyme is: Crotalus
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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
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hydrolysis of peptide bond
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Crotalus atrox metalloendopeptidase c
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hemorrhagic metalloproteinase HT-d
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Hemorrhagic toxin c and d
atrolysin
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Hemorrhagic toxin c and d
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Hemorrhagic toxin c and d
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red rattlesnake
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brenda
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brenda
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brenda
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SwissProt
brenda
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UniProt
brenda
rattlesnake
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brenda
Western diamondback rattlesnake
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brenda
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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
Acetyl-Val-Ala-Ala-Leu-Gly-Ala + 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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Basement membrane preparation + H2O
Soluble peptides
Basement membranes surrounding capillaries + H2O
?
bovine aggrecan monomer + H2O
?
cartilage aggrecan + H2O
?
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?
Collagen type IV + H2O
Hydrolyzed collagen type IV
Fibrinogen + H2O
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?
Fibrinogen + H2O
Hydrolyzed fibrinogen
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Fibronectin + H2O
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FSFRLT + H2O
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good substrate
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Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
Gelatin of collagen type III + H2O
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i.e. denatured collagen
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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 38ĆøC and above, not below
MW 130000, MW 118000, MW 93000 and MW 85000 fragments
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Glu-Ala-Leu-Tyr-Leu + H2O
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peptide derived from insulin B-chain
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hide powder azure + H2O
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HTLRKA + H2O
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good substrate
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?
Human alpha2-macroglobulin + H2O
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cleavage at Arg696-Leu697
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IAQLNR + H2O
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good substrate
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?
IPLRTV + H2O
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good substrate
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?
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
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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Nidogen + H2O
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basement membrane component
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Oxidized insulin B-chain + H2O
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SFMRLS + H2O
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good substrate
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?
TQRKRS + H2O
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good substrate
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?
Val-Glu-Ala-Leu-Tyr-Leu + H2O
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peptide derived from insulin B-chain
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von Willebrand factor + H2O
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additional information
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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
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?
Basement membrane preparation + H2O
Soluble peptides
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Basement membrane preparation + H2O
Soluble peptides
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poor substrate: component band a
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Basement membranes surrounding capillaries + H2O
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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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?
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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?
Collagen type IV + H2O
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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Dimethylcasein + H2O
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Dimethylcasein + H2O
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Gelatin of collagen type I + H2O
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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hide powder azure + H2O
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hide powder azure + H2O
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Laminin + H2O
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Laminin + H2O
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basement membrane component, poor substrate
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Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
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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Oxidized insulin B-chain + H2O
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Oxidized insulin B-chain + H2O
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cleavage at Gly23-Phe24
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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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cleavage at Gly23-Phe24
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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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von Willebrand factor + H2O
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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 fibrin
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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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no hydrolysis of peptide Ala-Leu-Tyr-Leu
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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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additional information
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hemorrhagic and myonecrotic activity
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Basement membranes surrounding capillaries + H2O
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von Willebrand factor + H2O
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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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Basement membranes surrounding capillaries + H2O
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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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Ca2+
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0.75 mol/mol toxin HT-3, 1.1 mol/mol toxin HT-2
Na+
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8.5 mol/mol toxin HT-3, 10.3 mol/mol toxin HT-2
additional information
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less than 0.3 mol Mg2+/mol toxin, less than 0.8 mol K+/mol toxin HT-3 and less than 0.9 mol K+/mol toxin HT-2
Zn2+
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1 mol zinc/mol enzyme; zinc metalloproteinase
Zn2+
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0.86 mol zinc/mol enzyme; zinc metalloproteinase
Zn2+
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zinc metalloproteinase
Zn2+
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zinc metalloprotease
Zn2+
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1 mol zinc/mol enzyme; zinc metalloproteinase
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Ala-Leu-Tyr-Leu
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isozyme Ht-c
amino acid hydroxymate
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Benzyloxycarbonyl-Leu-Gly-NHOH
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Collagenase inhibitor SC 44463
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Inhibitor SCH 47890
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mechanism
tissue inhibitor of metalloproteinase 3
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N-terminal domain of the tissue inhibitor of metalloproteinase 3 is a potent inhibitor
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1,10-phenanthroline
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1,10-phenanthroline
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inhibits proteolytic and hemorrhagic activity of atrolysin C
alpha2-Macroglobulin
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alpha2-Macroglobulin
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inhibits proteolytic and hemorrhagic activity of atrolysin C
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Amino acid hydroxamates
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Amino acid hydroxamates
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isozyme Ht-c
EDTA
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EDTA
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activity completely blocked
EDTA
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inhibits proteolytic and hemorrhagic activity of atrolysin C
phosphoramidon
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i.e. N-[L-rhamnopyranosyl-oxyhydroxyphosphinyl]-L-leucyl-L-tryptophan, isozyme Ht-c
phosphoramidon
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weak, isozyme Ht-d
phosphoramidon
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thermolysin inhibitor
additional information
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acetyl-Ala-Val-Leu-Gly-Ala, acetyl-Val-Glu-Leu-Gly-Ala, acetyl-Val-Lys-Leu-Gly-Ala, acetyl-Lys-Ala-Leu-Gly-Ala, acetyl-Val-Ala-Ile-Gly-Ala, furylacryloyl-Gly-L-Leu-NH2
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additional information
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no inhibition by aprotinin, PMSF
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additional information
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iodoacetate; no inhibition by aprotinin, PMSF
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additional information
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tissue inhibitor of metalloproteinase 1 and tissue inhibitor of metalloproteinase 2 have no inhibitory activity
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additional information
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inhibitory protein in the serum of Bothrops jararaca
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additional information
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the isolated recombinant cysteine-rich domain of atrolysin A does not inhibit full-length atrolysin activity, overview
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additional information
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benzamidine, tosyl-L-Phe chloromethyl ketone, soybean or egg white trypsin inhibitor or PCMB
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0.71
acetyl-Ala-Ala-Leu-Gly-Ala
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0.76
acetyl-Glu-Ala-Leu-Gly-Ala
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isozyme Ht-c
0.69
Acetyl-Val-Ala-Ala-Leu-Gly-Ala
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isozyme Ht-d
0.31 - 0.45
acetyl-Val-Ala-Leu-Gly-Gly
0.62 - 0.63
Acetyl-Val-Ala-Leu-Leu-Ala
0.5
acetyl-Val-Ala-Phe-Gly-Ala
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isozyme Ht-c
0.21
acetyl-Val-Gly-Leu-Gly-Ala
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isozyme Ht-c
0.14 - 0.29
Glu-Ala-Leu-Tyr-Leu
0.032 - 0.11
Leu-Val-Glu-Ala-Leu-Tyr-Leu
0.023 - 0.12
Val-Glu-Ala-Leu-Tyr-Leu
0.31
acetyl-Val-Ala-Leu-Gly-Gly
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isozyme c, acetyl-Val-Ala-Leu-Gly-Ala, 2-aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide
0.45
acetyl-Val-Ala-Leu-Gly-Gly
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isozyme Ht-c
0.62
Acetyl-Val-Ala-Leu-Leu-Ala
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acetyl-Val-Ala-Ala-Leu-Gly-Ala, isozyme Ht-c
0.63
Acetyl-Val-Ala-Leu-Leu-Ala
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isozyme Ht-d
0.14
Glu-Ala-Leu-Tyr-Leu
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isozyme Ht-d
0.29
Glu-Ala-Leu-Tyr-Leu
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isozyme Ht-c
0.032
Leu-Val-Glu-Ala-Leu-Tyr-Leu
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isozyme Ht-d
0.11
Leu-Val-Glu-Ala-Leu-Tyr-Leu
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isozyme Ht-c
0.023
Val-Glu-Ala-Leu-Tyr-Leu
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isozyme Ht-d
0.12
Val-Glu-Ala-Leu-Tyr-Leu
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isozyme Ht-c
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0.00015
tissue inhibitor of metalloproteinase 3
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8.3
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hide powder azure, isozyme Ht-c
9
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hide powder azure, isozyme Ht-d
additional information
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pI: 6 (isozyme Cc), pI: 6.1 (isozyme Cd)
additional information
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pI: 6 (isozyme Cc), pI: 6.1 (isozyme Cd)
additional information
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pI: 6.1 (isozyme Ht-d); pI: 6.2 (isozyme Ht-c)
additional information
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pI: 5.2 (toxin HT-2), pI: 9.6 (toxin HT-3)
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7.3 - 10
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about half-maximal activity at pH 7.3 and 10, isozyme Ht-d
7.5 - 9.8
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about half-maximal activity at pH 7.5 and 9.8, isozyme Ht-c
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37
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assay at
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31259 , 31260 , 31261 , 31265 , 31266 , 31268 , 31269 , 668846 , 670958 , 683459 , 734329
brenda
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brenda
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brenda
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brenda
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P15167
Crotalus atrox;
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20500
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Crotalus atrox, isozyme Ht-c, gel filtration
21000
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Crotalus atrox, isozyme Ht-d, gel filtration
23230
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Crotalus atrox, isozyme Ht-d
25000
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1 * 25000, Crotalus ruber ruber, toxin HT-2
25500
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1 * 25500, Crotalus ruber ruber, toxin HT-3
27900
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Crotalus atrox, minimal MW calculated from zinc content
24000
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1 * 24000, Crotalus atrox
additional information
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they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
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amino acid composition
additional information
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amino acid composition; isozymes Cc and Cd share identical antigenic structures
additional information
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amino acid composition; they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
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amino acid composition; amino acid sequence (81% identity of toxins HT-2 and Ht-d)
additional information
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amino acid composition
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monomer
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1 * 24000, Crotalus atrox; SDS-PAGE
monomer
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Crotalus ruber ruber, toxin HT-2; SDS-PAGE
monomer
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1 * 25000, Crotalus ruber ruber, toxin HT-2; 1 * 25500, Crotalus ruber ruber, toxin HT-3
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additional information
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no glycoprotein
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Crotalus atrox, crystallographic parameters
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X-ray structure of atrolysin C, form D
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formerly Ht-c and Ht-d; from lyophilized crude venom; two isozymes Cc and Cd
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from lyophilized crude venom
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from lyophilized crude venom, toxins HT-2 and HT-3
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gel filtration, ion exchange chromatography
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additional information
molecular characteristics that influence the toxic effects of snake venom metalloproteases, subdivision in hemorrhagic and non-hemorrhagic snake venom metalloproteases
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VM1AD_CROAT
414
46845
Swiss-Prot
VM1AC_CROAT
414
46769
Swiss-Prot
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Fox, J.W.; Bjarnason, J.B.
Atrolysins: metalloproteinases from Crotalus atrox venom
Methods Enzymol.
248
368-387
1995
Crotalus atrox
brenda
Bjarnason, J.B.; Hamilton, D.; Fox, J.W.
Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom
Biol. Chem. Hoppe-Seyler
369
121-129
1988
Crotalus atrox
brenda
Bjarnason, J.B.; Tu, A.T.
Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e
Biochemistry
17
3395-3404
1978
Crotalus atrox
brenda
Fox, J.W.; Campbell, R.; Beggerly, L.; Bjarnason, J.B.
Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom
Eur. J. Biochem.
156
65-72
1986
Crotalus atrox
brenda
Bjarnason, J.B.; Fox, J.W.
Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom
Biochim. Biophys. Acta
911
356-363
1987
Crotalus atrox
brenda
Shannon, J.D.; Baramova, E.N.; Bjarnason, J.B.; Fox, J.W.
Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin
J. Biol. Chem.
264
11575-11583
1989
Crotalus atrox
brenda
Zhang, D.; Botos, I.; Gomis-Ruth, F.X.; Doll, R.; Blood, C.; Njoroge, F.G.; Fox, J.W.; Bode, W.; Meyer, E.F.
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)
Proc. Natl. Acad. Sci. USA
91
8447-8451
1994
Crotalus atrox
brenda
Takeya, H.; Onikura, A.; Nikai, T.; Sugihara, H.; Iwanaga, S.
Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber
J. Biochem.
108
711-719
1990
Crotalus ruber ruber
brenda
Mori, N.; Nikali, T.; Sugihara, H.; Tu, A.T.
Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom
Arch. Biochem. Biophys.
253
108-121
1987
Crotalus ruber ruber
brenda
Tortorella, M.D.; Pratta, M.A.; Fox, J.W.; Arner, E.C.
The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites
J. Biol. Chem.
273
5846-5850
1998
Crotalus atrox
brenda
Pinto, A.F.; Terra, R.M.; Guimaraes, J.A.; Kashiwagi, M.; Nagase, H.; Serrano, S.M.; Fox, J.W.
Structural features of the reprolysin atrolysin C and tissue inhibitors of metalloproteinases (TIMPs) interaction
Biochem. Biophys. Res. Commun.
347
641-648
2006
Crotalus atrox
brenda
Fox, J.W.
Atrolysin C
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
671-673
2004
Crotalus atrox
-
brenda
Ramos, O.H.; Selistre-de-Araujo, H.S.
Comparative analysis of the catalytic domain of hemorrhagic and non-hemorrhagic snake venom metallopeptidases using bioinformatic tools
Toxicon
44
529-538
2004
Crotalus atrox (P15167)
brenda
Serrano, S.M.; Wang, D.; Shannon, J.D.; Pinto, A.F.; Polanowska-Grabowska, R.K.; Fox, J.W.
Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation
FEBS J.
274
3611-3621
2007
Crotalus atrox
brenda
Dagda, R.K.; Gasanov, S.E.; Zhang, B.; Welch, W.; Rael, E.D.
Molecular models of the Mojave rattlesnake (Crotalus scutulatus scutulatus) venom metalloproteinases reveal a structural basis for differences in hemorrhagic activities
J. Biol. Phys.
40
193-216
2014
Crotalus atrox, Crotalus atrox (Q90392), Crotalus scutulatus scutulatus
brenda
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