Aminopeptidase activity in adult Schistosoma mansoni.
An aminopeptidase activity capable of hydrolysing leucine 4-nitroanilide and alanine 4-nitroanilide at pH 7.0 was detected in saponin-CaCl2 extracts and homogenates of adult Schistosoma mansoni. The extracts were also capable of acting on synthetic dipeptides at the same pH, preferentially hydrolysing peptide bonds following leucine, alanine, or proline N-terminal residues. Imide bonds were not hydrolysed. The hydrolysis of leucine 4-nitroanilide was apparently stimulated by thiols, strongly inhibited by 1 mM 4-chloromercuric benzene sulfonic acid, and partially inhibited by 1 mM 1,10-phenanthroline.
D002731:4-Chloromercuribenzenesulfonate / Q000494:pharmacology; D000626:Aminopeptidases / Q000378:metabolism*; D000813:Anilides / Q000378:metabolism; D000818:Animals; D002412:Cations / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000378:metabolism; D005260:Female; D006863:Hydrogen-Ion Concentration; D008297:Male; D010618:Phenanthrolines / Q000494:pharmacology; D012550:Schistosoma mansoni / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D000813:Anilides; D002412:Cations; D010618:Phenanthrolines; D013438:Sulfhydryl Compounds; D002731:4-Chloromercuribenzenesulfonate; C001536:1-leucine-4-nitroanilide; D010450:Endopeptidases; D000626:Aminopeptidases; C025205:1,10-phenanthroline