Primary specificity of ancrod, the coagulating serine proteinase from the Malayan pit viper (Agkistrodon rhodostoma) venom.
Values of steady-state and pre-steady-state parameters for the hydrolysis of ZArgONp and ZLysONp catalysed by ancrod, the coagulating serine proteinase from the Malayan pit viper (Agkistrodon rhodostoma) venom, have been determined, between pH 2.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C, and analysed in parallel with those of bovine alpha-thrombin and porcine pancreatic beta-kallikrein-B. In addition to the well-known coagulating behaviour, ancrod also shows catalytic properties, in the hydrolysis of ZArgONp and ZLysONp, reminiscent of those of porcine pancreatic beta-kallikrein-B.
D000721:Ancrod / Q000378:metabolism*; D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism; D003435:Crotalid Venoms / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007610:Kallikreins / Q000378:metabolism; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives / Q000378:metabolism; D013379:Substrate Specificity; D013917:Thrombin / Q000378:metabolism
C031442:Agkistrodon venoms; D003435:Crotalid Venoms; C040761:N-benzyloxycarbonylarginine 4-nitrophenyl ester; C034117:N-benzyloxycarbonyllysine 4-nitrophenyl ester; D001120:Arginine; D000721:Ancrod; D007610:Kallikreins; D013917:Thrombin; D008239:Lysine