CRYSTALLINE ENZYME-KINETICS - ACTIVITY OF THE STREPTOMYCES R61 D-ALANYL-D-ALANINE PEPTIDASE

被引：9

作者：

KELLY, JA

WALEY, SG

ADAM, M

FRERE, JM

机构：

[1] LAB MOLEC BIOPHYS,OXFORD,ENGLAND

[2] UNIV OXFORD,OXFORD CTR MOLEC SCI,OXFORD,ENGLAND

[3] UNIV OXFORD,SIR WILLIAM DUNN SCH PATHOL,OXFORD OX1 3RE,ENGLAND

[4] STATE UNIV LIEGE,FAC MED,INST CHIM,SERV MICROBIOL,B-4000 LIEGE,BELGIUM

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1119卷 / 03期

关键词：

ENZYME KINETICS; CRYSTALLINE KINETICS; D-ALANYL-D-ALANINE PEPTIDASE; 4,4'-DITHIODIPYRIDINE-COUPLED REACTION; HIPPURYL-MERCAPTOACETIC ACID;

D O I：

10.1016/0167-4838(92)90211-U

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：

The specificity constant, k(cat)/K(m) for the hydrolysis of hippuyl-mercaptoacetate by crystals of the Streptomyces R61 D-D peptidase was measured by reaction of the thiol produced with 4,4'-dithiodipyridine. The values of k(cat)/K(m) for the crystal and in solution were the same (within experimental error). A novel method for treating the lag in the progress curves was developed.

引用

页码：256 / 260

页数：5

共 18 条

[1] CHROMOGENIC DEPSIPEPTIDE SUBSTRATES FOR BETA-LACTAMASES AND PENICILLIN-SENSITIVE DD-PEPTIDASES [J].