Proteolytic specificity of moojeni protease A isolated from the venom of Bothrops moojeni.
Moojeni protease A, a proteolytic enzyme isolated from Bothrops moojeni venom, hydrolyzes type I collagen, gelatin, fibrinogen, fibrin and the B-chain of oxidized insulin. The proteinase cleaves the A alpha-chain faster than the B beta-chain of human fibrinogen and shows no effect on the gamma-chain. Fibrin solubilization appears to occur from the hydrolysis of the alpha-polymer and unpolymerized alpha-chain. The enzyme cleaves the Ala(14)-Leu(15) bond of the oxidized insulin B-chain most rapidly, followed by splitting the Ser(9)-His(10) bond. The Tyr(16)-Leu(17) and Gly(20)-Glu(21) cleavage sites were hydrolyzed slightly more slowly, while the peptide bonds His(5)-Leu(6), His(10)-Leu(11), Glu(21)-Arg(22), Gly(23)-Phe(24) and Phe(24)-Phe(25) were more resistant to the enzyme attack. Small synthetic peptides were not hydrolyzed by moojeni protease A.
Reichl
A P
AP
Serviço de Bioquímica, Instituto Butantan, São Paulo, Brazil.
Mandelbaum
F R
FR
D000595:Amino Acid Sequence; D003094:Collagen / Q000378:metabolism; D003435:Crotalid Venoms / Q000201:enzymology*; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D005780:Gelatin / Q000378:metabolism; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism; D008666:Metalloendopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D013379:Substrate Specificity
D003435:Crotalid Venoms; D007328:Insulin; D010455:Peptides; D005780:Gelatin; D005337:Fibrin; D005340:Fibrinogen; D003094:Collagen; C046860:Bothrops moojeni protease A; D008666:Metalloendopeptidases