Characterization of a carboxypeptidase from the yeast Rhodotorula glutinis.
A carboxypeptidase has been identified in Rhodotorula glutinis and partially purified. The enzyme is active on N-substituted dipeptides and tripeptides and also exhibits an esterolytic activity. Both activities are inhibited by (N-benzyloxycarbonyl-L-phenylalanyl)chloromethane and by a thermostable fraction present in extracts. The enzyme shows a pH optimum in the range 7.5 to 8.0 and has a molecular weight of 80000, determined by gel filtration.
D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D012248:Rhodotorula / Q000201:enzymology*; D013379:Substrate Specificity
D002268:Carboxypeptidases