The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31.
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.
Takano
R
R
Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology.
Imada
C
C
Kamei
K
K
Hara
S
S
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*
D009842:Oligopeptides; D011480:Protease Inhibitors; C073224:marinostatin D; D002918:Chymotrypsin