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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
-
-
-
-
?
acetyl-Ala-Ala-Leu-Gly-Ala + H2O
?
-
-
-
-
?
acetyl-Glu-Ala-Leu-Gly-Ala + H2O
?
-
-
-
-
?
Acetyl-Val-Ala-Ala-Leu-Gly-Ala + H2O
?
-
-
-
-
?
acetyl-Val-Ala-Leu-Gly-Gly + H2O
?
-
-
-
-
?
Acetyl-Val-Ala-Leu-Leu-Ala + H2O
?
-
best substrate of synthetic acetylated pentapeptides
-
-
?
acetyl-Val-Ala-Phe-Gly-Ala + H2O
?
-
-
-
-
?
acetyl-Val-Gly-Leu-Gly-Ala + H2O
?
-
-
-
-
?
Basement membrane preparation + H2O
Soluble peptides
Basement membranes surrounding capillaries + H2O
?
bovine aggrecan monomer + H2O
?
cartilage aggrecan + H2O
?
-
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
Dimethylcasein + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
Hydrolyzed fibrinogen
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
FSFRLT + H2O
?
-
good substrate
-
-
?
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
Gelatin of collagen type III + H2O
?
-
i.e. denatured collagen
-
-
?
Gelatin of collagen type V + H2O
Hydrolyzed gelatin of collagen type V
-
i.e. denatured collagen, hydrolysis at 38øC and above, not below
MW 130000, MW 118000, MW 93000 and MW 85000 fragments
?
Glu-Ala-Leu-Tyr-Leu + H2O
?
-
peptide derived from insulin B-chain
-
-
?
hide powder azure + H2O
?
-
-
-
-
?
HTLRKA + H2O
?
-
good substrate
-
-
?
Human alpha2-macroglobulin + H2O
?
-
cleavage at Arg696-Leu697
-
-
?
IAQLNR + H2O
?
-
good substrate
-
-
?
IPLRTV + H2O
?
-
good substrate
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
Nidogen + H2O
?
-
basement membrane component
-
-
?
Oxidized insulin B-chain + H2O
?
SFMRLS + H2O
?
-
good substrate
-
-
?
TQRKRS + H2O
?
-
good substrate
-
-
?
Val-Glu-Ala-Leu-Tyr-Leu + H2O
?
-
peptide derived from insulin B-chain
-
-
?
von Willebrand factor + H2O
?
additional information
?
-
Basement membrane preparation + H2O
Soluble peptides
-
-
-
-
?
Basement membrane preparation + H2O
Soluble peptides
-
poor substrate: component band a
-
?
Basement membranes surrounding capillaries + H2O
?
-
involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
-
-
?
Basement membranes surrounding capillaries + H2O
?
-
together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
-
-
?
Basement membranes surrounding capillaries + H2O
?
-
together with atrolysins B and E member of the class P-I hemorrhagic toxins
-
-
?
Basement membranes surrounding capillaries + H2O
?
-
less potent hemorrhagic toxins of Crotalus atrox venom
-
-
?
bovine aggrecan monomer + H2O
?
-
-
-
?
bovine aggrecan monomer + H2O
?
-
purified atrolysin C can cleave at the cleavage sites VIPEN + FFBVG and ITEGE + ARGSV independently
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
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
?
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
-
i.e. denatured collagen
-
-
?
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
-
i.e. denatured collagen
MW 60000 and MW 50000 fragments
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
basement membrane component, poor substrate
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
-
cleavage at Ala-Leu
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
-
peptide derived from insulin B-chain, best substrate
-
-
?
Oxidized insulin B-chain + H2O
?
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage at Gly23-Phe24
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage at His5-Leu6, His10-Leu11, Ala14-Leu15 (most rapidly cleaved bond)
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleaves the same bonds as atrolysin B and A (the latter except Gly23-Phe24)
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage at Tyr16-Leu17 (slightly less rapidly cleaved bond)
-
-
?
von Willebrand factor + H2O
?
-
VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
-
-
?
von Willebrand factor + H2O
?
-
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
-
-
?
additional information
?
-
-
no hydrolysis of fibrin
-
-
?
additional information
?
-
-
no hydrolysis of interstitial collagen, native type I collagen
-
-
?
additional information
?
-
-
no hydrolysis of peptide Ala-Leu-Tyr-Leu
-
-
?
additional information
?
-
-
cleavage specificity, compared to hemorrhagic toxins a and b
-
-
?
additional information
?
-
-
substrate requirements: small aliphatic residues at P1 (Ala or Gly) and Leu at P2
-
-
?
additional information
?
-
-
substrate digestion patterns differ from those of atrolysins A and E
-
-
?
additional information
?
-
-
peptides of four residues or less are not hydrolyzed, no significant degradation of fibrin
-
-
?
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Ala-Leu-Tyr-Leu
-
isozyme Ht-c
amino acid hydroxymate
-
-
Benzyloxycarbonyl-Leu-Gly-NHOH
-
-
Collagenase inhibitor SC 44463
-
-
Inhibitor SCH 47890
-
mechanism
tissue inhibitor of metalloproteinase 3
-
N-terminal domain of the tissue inhibitor of metalloproteinase 3 is a potent inhibitor
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
alpha2-Macroglobulin
-
-
-
alpha2-Macroglobulin
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
-
Amino acid hydroxamates
-
-
Amino acid hydroxamates
-
isozyme Ht-c
EDTA
-
-
EDTA
-
activity completely blocked
EDTA
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
phosphoramidon
-
weak, isozyme Ht-d
phosphoramidon
-
i.e. N-[L-rhamnopyranosyl-oxyhydroxyphosphinyl]-L-leucyl-L-tryptophan, isozyme Ht-c
phosphoramidon
-
thermolysin inhibitor
additional information
-
iodoacetate
-
additional information
-
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
-
additional information
-
no inhibition by aprotinin, PMSF
-
additional information
-
no inhibition by aprotinin, PMSF
-
additional information
-
inhibitory protein in the serum of Bothrops jararaca
-
additional information
-
tissue inhibitor of metalloproteinase 1 and tissue inhibitor of metalloproteinase 2 have no inhibitory activity
-
additional information
-
the isolated recombinant cysteine-rich domain of atrolysin A does not inhibit full-length atrolysin activity, overview
-
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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
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 (Q90392), Crotalus atrox, Crotalus scutulatus scutulatus
brenda