Amino acid sequence around the active site aspartic acid in penicillopepsin

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Abstract
Penicillopepsin, the acid proteinase of Penicillium janthinellum, was specifically inactivated with diazoacetylnorleucine methyl ester. The peptide containing the glycollylnorleucine methyl ester group was isolated from a peptic digest. The amino acid sequence was found to be Ile∙Ala∙β(glycollyl-Nle OMe)-Asp∙Thr∙Gly∙Thr∙Thr∙Leu and is thus almost identical with the active site peptide of porcine pepsin: Ile∙Val∙Asp∙Thr∙Gly∙Thr∙Ser. This finding provides strong evidence for an evolutionary homology between penicillopepsin and porcine pepsin.

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