Amino Acid Sequences around 1, 2-Epoxy-3-(p-nitrophenoxy)propane-reactive Residues in Rhizopus chinensis Acid Protease: Homology with Pepsin and Rennin

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Abstract
Two different peptides containing an aspartyl residue reactive with 1,2-epoxy-3-(p-nitro-phenoxy)propane (EPNP) in the acid protease from Rhizopus chinensis were isolated from a peptic digest of the EPNP-modified enzyme. One of the peptides was sequenced as Asp-Thr-Gly-Ser-Ser-Asp. The amino acid sequence had very high homology with those around the EPNP-reactive aspartyl residues in rennin (chymosin) [EC 3.4.23.4] and pepsin [EC 3.4.23.1]. The other peptide contained no methionine residue and gave the sequence: [Asp-Thr-Gly-Thr-Thr-Leu. The N-terminal aspartyl residue of each peptide was deduced to be the EPNP-reactive site.