Amino acid sequences around 1, 2-epoxy-3-(p-nitrophenoxy)propane-reactive residues in rhizopus chinensis acid protease: homology with pepsin and rennin.
Two different peptides containing an aspartyl residue reactive with 1, 2-epoxy-3-(p-nitrophenoxy)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-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.
D000595:Amino Acid Sequence; D001665:Binding Sites; D012085:Chymosin; D004852:Epoxy Compounds; D006863:Hydrogen-Ion Concentration; D009596:Nitrophenols; D010434:Pepsin A; D010447:Peptide Hydrolases; D011485:Protein Binding; D012233:Rhizopus / Q000201:enzymology*; D013329:Structure-Activity Relationship
D004852:Epoxy Compounds; D009596:Nitrophenols; D010447:Peptide Hydrolases; D010434:Pepsin A; D012085:Chymosin