Action of yeast proteinase C on synthetic peptides and poly-α,l-amino acids

摘要: Abstract Yeast proteinase C liberates carboxy-terminal amino acids from a wide variety of N-acyl dipeptides which have aromatic, neutral, acidic or basic acid in the end. Noticeably, internal proline peptides can also be liberated. The enzyme has esterase activity for N- acetyl- l -tyrosine ethyl ester and amidase carbobenzoxy dipeptide amides. rapidly hydrolyses poly-α, -glutamic at pH 4.2, liberating only glutamic acid, while poly- -lysine -proline are never hydrolysed. All these activities powerfully inhibited by p-chloromercuribenzoate (PCMB) DFP. Poly- inhibits both peptidase carbobenzoxy-Glu-Tyr ester.