EC Number   |
General Information |
Reference |
|---|
   3.4.24.1 | evolution |
the Crotalus atrox metalloproteinase (CAMP) is a group III metalloprotease showing high similarity to VAP2A |
755070 |
| 3.4.24.1 | metabolism |
the enzyme is regulated by heme |
752921 |
| 3.4.24.1 | more |
the snake venom metalloproteinase is heme-bound and CO-inhibited |
752921 |
| 3.4.24.1 | 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 |
754464 |
| 3.4.24.1 | physiological function |
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 |
735314 |
| 3.4.24.1 | physiological function |
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 |
755070 |
