The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31

J Biochem. 1991 Dec;110(6):856-8. doi: 10.1093/oxfordjournals.jbchem.a123678.

Abstract

A new homologue of marinostatin, a peptide proteinase inhibitor, was isolated from marine Alteromonas sp. B-10-31 and designated as marinostatin D. Its amino acid sequence was determined to be Ala-Thr-Met-Arg-Tyr-Pro-Ser-Asp-Asp-Ser-Glu. The reactive site of marinostatin D was determined to be Met(3)-Arg(4) on the basis of the reversible cleavage and regeneration of the scissile bond catalyzed by TLCK-chymotrypsin.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Chymotrypsin
  • Gram-Negative Aerobic Bacteria / chemistry*
  • Molecular Sequence Data
  • Oligopeptides / chemistry*
  • Protease Inhibitors / chemistry*

Substances

  • Oligopeptides
  • Protease Inhibitors
  • marinostatin D
  • Chymotrypsin