THE REACTIVE SITE OF MARINOSTATIN, A PROTEINASE-INHIBITOR FROM MARINE ALTEROMONAS SP B-10-31

被引：15

作者：

TAKANO, R

IMADA, C

KAMEI, K

HARA, S ^{[1
]}

机构：

[1] KYOTO INST TECHNOL,FAC ENGN & DESIGN,DEPT CHEM & MAT TECHNOL,SAKYO KU,KYOTO 606,JAPAN

[2] INST MICROBIAL CHEM,SHINAGAWA KU,TOKYO 141,JAPAN

来源：

JOURNAL OF BIOCHEMISTRY | 1991年 / 110卷 / 06期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a123678

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：856 / 858

页数：3

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