Isolation and Amino Acid Sequence of a Peptide Containing an Epoxide-Reactive Residue From the Thermolysin-Digest of Scytalidium Lignicolum Acid Protease B

J Biochem. 1986 May;99(5):1537-9. doi: 10.1093/oxfordjournals.jbchem.a135624.


Scytalidium lignicolum acid protease B, a pepstatin-insensitive acid protease, was modified by 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP) with the concomitant loss of its enzyme activity, and an EPNP-labeled peptide was isolated from the thermolysin-digest of the modified enzyme by HPLC. The amino acid sequence of the peptide was determined to be Ile-Leu-Glu-Thr-Gly, which corresponds to the sequence of residue Nos. 51-55 of the enzyme. The results of treatment of the labeled peptide with hydroxylamine suggested that the EPNP moiety is ester-linked to Glu53 of the enzyme. The amino acid sequence around Glu53 of the acid protease B showed high homology with those around the active site Asp residues of calf chymosin and porcine pepsin. These results show that it is highly possible that Glu53 of the acid protease B is one of the amino acid residues involved in its catalytic activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aspartic Acid Endopeptidases*
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Endopeptidases*
  • Epoxy Compounds
  • Hydrolysis
  • Mitosporic Fungi / enzymology*
  • Nitrophenols*
  • Peptide Fragments / isolation & purification
  • Thermolysin


  • Epoxy Compounds
  • Nitrophenols
  • Peptide Fragments
  • 1,2-epoxy-3-(p-nitrophenoxy)propane
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • Scytalidium lignicolum acid proteases
  • Thermolysin