3.4.24.1: atrolysin A
This is an abbreviated version!
For detailed information about atrolysin A, go to the full flat file.
Word Map on EC 3.4.24.1
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3.4.24.1
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thrombospondin
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metalloproteinases
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integrins
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adamts
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collagen
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platelet
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endothelial
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cartilage
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thrombotic
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ectodomains
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willebrand
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aggrecan
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chondrocytes
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thrombocytopenic
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purpura
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osteoarthritis
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articular
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rgd
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ttp
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cysteine-rich
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proteoglycans
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sheddase
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membrane-anchored
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viper
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alphavbeta3
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alpha-secretase
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aggrecanase
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timp-3
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arg-gly-asp
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microangiopathic
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adamts-13
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trimeresurus
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rgd-containing
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svmps
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hb-egf
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envenom
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echis
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carinatus
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versican
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metzincins
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metalloproteinase-13
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schistocytes
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prodomains
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sperm-egg
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medicine
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bothrops
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viperidae
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agkistrodon
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alphaiibbeta3
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rattlesnake
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non-amyloidogenic
- 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
Reaction
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
atrolysin-e, Cam-dis, CAMP, CatroxMP-II, CaVMP-II, crotalus atrox alpha-proteinase, crotalus atrox metalloproteinase, crotalus atrox proteinase, crotalus atrox.alpha.-proteinase, Crotatroxin, disintegrin, fibrinogenolytic metalloproteinase, hemorrhagic toxin a, proteinase, Crotalus atrox, snake venom disintegrin, snake venom metalloprotease, snake venom metalloproteinase, SVMP, zinc metalloproteinase-disintegrin VMP-II
ECTree
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General Information
General Information on EC 3.4.24.1 - atrolysin A
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evolution
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the Crotalus atrox metalloproteinase (CAMP) is a group III metalloprotease showing high similarity to VAP2A
physiological function
additional information
recombinant protease inhibits platelet adhesion to fibrinogen with an estimated IC50 of 1 nM. It inhibits collagen- (IC50 is 18 nM) and ADP-induced (IC50 is 6 nM) platelet aggregation, and also inhibits platelet function on clot retraction
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
the snake venom metalloproteinase is heme-bound and CO-inhibited
additional information
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the snake venom metalloproteinase is heme-bound and CO-inhibited