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Information on EC 3.4.24.1 - atrolysin A and Organism(s) Crotalus atrox and UniProt Accession C9E1R7
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3.4.24.1 atrolysin ASpecify your search results
Word Map
- 3.4.24.1
- thrombospondin
- metalloproteinases
- integrins
-
adamts
- collagen
- platelet
- endothelial
- cartilage
-
thrombotic
- ectodomains
- willebrand
- aggrecan
- chondrocytes
-
thrombocytopenic
- purpura
- osteoarthritis
-
articular
- rgd
- ttp
-
cysteine-rich
- proteoglycans
- sheddase
-
membrane-anchored
- viper
- alphavbeta3
- alpha-secretase
- aggrecanase
- timp-3
- arg-gly-asp
-
microangiopathic
- adamts-13
- trimeresurus
-
rgd-containing
-
svmps
- hb-egf
-
envenom
- echis
- carinatus
- versican
-
metzincins
- metalloproteinase-13
-
schistocytes
- prodomains
-
sperm-egg
- medicine
- bothrops
- viperidae
- agkistrodon
- alphaiibbeta3
- rattlesnake
-
non-amyloidogenic
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 Asn3-/-Gln, His5-/-Leu, His10-/-Leu, Ala14-/-Leu and Tyr16-/-Leu in insulin B chain; removes C-terminal Leu from small peptides
Synonyms
disintegrin, snake venom disintegrin, snake venom metalloprotease, atrolysin a, crotatroxin, fibrinogenolytic metalloproteinase, crotalus atrox alpha-proteinase, hemorrhagic toxin a, cavmp-ii, catroxmp-ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
crotalus atrox alpha-proteinase
-
-
-
-
crotalus atrox metalloproteinase
crotalus atrox proteinase
-
-
-
-
crotalus atrox.alpha.-proteinase
-
-
-
-
hemorrhagic toxin a
-
-
-
-
proteinase, Crotalus atrox
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-
-
-
SVMP
crotalus atrox metalloproteinase
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-82-7
-
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
insulin B chain + H2O
?
-
cleaves Ala14-Leu15 bond of insulin B chain most rapidly
-
-
?
Nalpha-benzoyl-L-arginine-7-amido-4-methylcoumarin + H2O
Nalpha-benzoyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Proteins + H2O
?
-
preferential cleavage: -Leu, -Ile, -Val, -Phe
-
-
?
Type I collagen + H2O
?
-
enzyme binds via exosites in the cysteine-rich domain
-
-
?
von Willebrand factor + H2O
?
-
enzyme binds via exosites in the cysteine-rich domain
-
-
?
additional information
?
-
-
the recombinant cysteine-rich domain of the enzyme has the ability to inhibit collagen-stimulated platelet aggregation
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CORM-2
a tricarbonyldichlororuthenium (II) dimer, and a CO releasing molecule, inhibits the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma via CO
-
additional information
-
not: phenylmethanesulfonyl fluoride, Nalpha-p-tosyl-L-phenylalanine chloromethyl ketone, Nalpha-p-tosyl-L-lysine chloromethyl ketone
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the Crotalus atrox metalloproteinase (CAMP) is a group III metalloprotease showing high similarity to VAP2A
physiological function
additional information
physiological function
disintegrin Crotatroxin from venom of Crotalus atrox has targets within the coagulation cascade, including receptors on platelets. The disintegrin from venom can attenuates hemorrhagic transformation by preventing activation of matrix metalloproteinase-9 after middle cerebral artery occlusion (MCAO) in hyperglycemic male Sprague-Dawley rats
physiological function
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snake venom metalloproteases (SVMPs) are a predominant component of viper venoms, and are involved in the degradation of basement membrane proteins (particularly collagen) surrounding the tissues around the bite site. Crotalus atrox metalloprotease (CAMP) displays both collagenolytic and fibrinogenolytic activities and inhibits CRP-XL-induced platelet aggregation. Permanent muscle damage induced by snake venom metalloprotease on tibialis anterior muscle of C57BL/6 mice, mechanism, overview. CAMP significantly damages skeletal muscles by attacking the collagen scaffold and other important basement membrane proteins, and prevents their regeneration through disrupting the functions of satellite cells. CAMP extensively damages the extracellular matrix surrounding the myofibres
additional information
the snake venom metalloproteinase is heme-bound and CO-inhibited
additional information
-
the snake venom metalloproteinase is heme-bound and CO-inhibited
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
trypsin peptide mapping and mass spectrometric analysis
additional information
-
trypsin peptide mapping and mass spectrometric analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from venom by anion exchange chromatography and gel filtration
-
native enzyme from venom by anion exchange chromatography, dialysis, ultrafiltration, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of recombinant cysteine-rich domain of atrolysin A in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
disintegrins found in Crotalus atrox venom may have therapeutic potential for reducing hemorrhagic transformation after ischemic stroke
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Kruzel, M.; Kress, L.F.
Separation of Crotalus atrox (western diamondback rattlesnake) alpha-proteinase from serine proteinase and hemorrhagic factor activities
Anal. Biochem.
151
471-478
1985
Crotalus atrox
Baramova, E.N.; Shannon, J.D.; Bjarnason, J.B.; Fox, J.W.
Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases
Arch. Biochem. Biophys.
275
63-71
1989
Crotalus atrox
Baramova, E.N.; Shannon, J.D.; Bjarnason, J.B.; Gonias, S.L.; Fox, J.W.
Interaction of hemorrhagic metalloproteinases with human alpha 2-macroglobulin
Biochemistry
29
1069-1074
1990
Crotalus atrox
Komori, Y.; Hagihara, S.; Tu, A.T.
Specificity of hemorrhagic proteinase from Crotalus atrox (western diamondback rattlesnake) venom
Biochim. Biophys. Acta
829
127-130
1985
Crotalus atrox
Chiou, S.H.; Hung, C.C.; Lin, C.W.
Isolation of a crotalase-like protease with alpha-fibrinogenase activity from the western diamondback rattlesnake, Crotalus atrox
Biochem. Int.
26
105-112
1992
Crotalus atrox
Patston, P.A.; Qi, M.; Schifferli, J.A.; Schapira, M.
The effect of cleavage by a Crotalus atrox alpha-proteinase fraction on the properties of C1-inhibitor
Toxicon
33
53-61
1995
Crotalus atrox
Chiou, S.H.; Hung, C.C.; Huang, K.F.
Characterization of a protease with alpha- and beta-fibrinogenase activity from the Western diamondback rattlesnake, Crotalus atrox
Biochem. Biophys. Res. Commun.
187
389-396
1992
Crotalus atrox
Jia L.G.; Wang, X.M.; Shannon, J.D.; Bjarnason, J.B.; Fox, J.W.
Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A
Arch. Biochem. Biophys.
373
281-286
2000
Crotalus atrox
Serrano, S.M.; Jia, L.G.; Wang, D.; Shannon, J.D.; Fox, J.W.
Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor
Biochem. J.
391
69-76
2005
Crotalus atrox
Pinto, A.F.; Ma, L.; Dragulev, B.; Guimaraes, J.A.; Fox, J.W.
Use of SILAC for exploring sheddase and matrix degradation of fibroblasts in culture by the PIII SVMP atrolysin A: identification of two novel substrates with functional relevance
Arch. Biochem. Biophys.
465
11-15
2007
Crotalus atrox
Jia, Y.; Prez, J.
Molecular cloning and characterization of cDNAs encoding metalloproteinases from snake venom glands
Toxicon
55
462-469
2010
Crotalus atrox (C9E1R7), Crotalus atrox
Suntravat, M.; Langlais, P.R.; Sanchez, E.E.; Nielsen, V.G.
CatroxMP-II a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom
Biometals
31
585-593
2018
Crotalus atrox (P34182), Crotalus atrox
McBride, D.W.; Gren, E.C.K.; Kelln, W.; Hayes, W.K.; Zhang, J.H.
Crotalus atrox disintegrin reduces hemorrhagic transformation by attenuating matrix metalloproteinase-9 activity after middle cerebral artery occlusion in hyperglycemic male rats
J. Neurosci. Res.
2018
1-11
2018
Crotalus atrox (P68520), Crotalus atrox
Williams, H.F.; Mellows, B.A.; Mitchell, R.; Sfyri, P.; Layfield, H.J.; Salamah, M.; Vaiyapuri, R.; Collins-Hooper, H.; Bicknell, A.B.; Matsakas, A.; Patel, K.; Vaiyapuri, S.
Mechanisms underpinning the permanent muscle damage induced by snake venom metalloprotease
PLoS Negl. Trop. Dis.
13
e0007041
2019
Crotalus atrox
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