title: The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31.
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.
authors.affiliation: Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology.
authors.forename: R
authors.initials: R
authors.lastname: Takano
authors.forename: C
authors.initials: C
authors.lastname: Imada
authors.forename: K
authors.initials: K
authors.lastname: Kamei
authors.forename: S
authors.initials: S
authors.lastname: Hara
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002918:Chymotrypsin; D006088:Gram-Negative Aerobic Bacteria / Q000737:chemistry*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011480:Protease Inhibitors / Q000737:chemistry*
chemical_list: D009842:Oligopeptides; D011480:Protease Inhibitors; C073224:marinostatin D; D002918:Chymotrypsin