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Information on EC 3.4.24.42 - atrolysin C and Organism(s) Crotalus atrox and UniProt Accession P15167
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3.4.24.42 atrolysin CSpecify your search results
Word Map
- 3.4.24.42
- cartilage
-
articular
- osteoarthritis
- joint
- chondrocytes
- proteoglycans
-
explants
- metalloproteinases
- collagen
- adamts-4
- glycosaminoglycans
- thrombospondin
- synovial
-
disintegrin
- knee
-
neoepitope
-
interglobular
-
arthritic
- mmp-1
-
aggrecanolysis
- chondroitin
-
aggrecan-degrading
- timp-3
-
nitege
- versican
-
disintegrin-like
- interleukin-1alpha
-
chondroprotective
- igd
-
matrix-degrading
- adamalysin
-
subchondral
-
meniscal
The taxonomic range for the selected organisms is: Crotalus atrox
The expected taxonomic range for this enzyme is: Crotalus
The expected taxonomic range for this enzyme is: Crotalus
Reaction Schemes
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 c, atrolysin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Crotalus atrox metalloendopeptidase c
-
-
-
-
Hemorrhagic toxin c and d
Ruberlysin
-
-
-
-
Hemorrhagic toxin c and d
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
158886-17-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
-
-
-
-
?
Acetyl-Val-Ala-Leu-Leu-Ala + H2O
?
-
best substrate of synthetic acetylated pentapeptides
-
-
?
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
?
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
?
-
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
?
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
?
-
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 interstitial collagen, native type I collagen
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
von Willebrand factor + H2O
?
-
VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tissue inhibitor of metalloproteinase 3
-
N-terminal domain of the tissue inhibitor of metalloproteinase 3 is a potent inhibitor
-
1,10-phenanthroline
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
alpha2-Macroglobulin
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
-
phosphoramidon
-
i.e. N-[L-rhamnopyranosyl-oxyhydroxyphosphinyl]-L-leucyl-L-tryptophan, isozyme Ht-c
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
acetyl-Val-Ala-Leu-Gly-Gly
-
isozyme c, acetyl-Val-Ala-Leu-Gly-Ala, 2-aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VM1AD_CROAT
414
0
46845
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
additional information
additional information
-
isozymes Cc and Cd share identical antigenic structures
additional information
-
they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
-
they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
molecular characteristics that influence the toxic effects of snake venom metalloproteases, subdivision in hemorrhagic and non-hemorrhagic snake venom metalloproteases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fox, J.W.; Bjarnason, J.B.
Atrolysins: metalloproteinases from Crotalus atrox venom
Methods Enzymol.
248
368-387
1995
Crotalus atrox
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
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
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
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
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
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
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
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
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
-
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)
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
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
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