Evidence from kinetic isotope studies for an enolate intermediate in the mechanism of type II dehydroquinases

被引：64

作者：

Harris, JM

GonzalezBello, C

Kleanthous, C

Hawkins, AR

Coggins, JR

Abell, C

机构：

[1] UNIV E ANGLIA, SCH BIOL SCI, NORWICH NR4 7TJ, NORFOLK, ENGLAND

[2] UNIV NEWCASTLE UPON TYNE, DEPT BIOCHEM & GENET, NEWCASTLE UPON TYNE NE2 4HH, TYNE & WEAR, ENGLAND

[3] UNIV GLASGOW, DEPT BIOCHEM, GLASGOW G12 8QQ, LANARK, SCOTLAND

来源：

BIOCHEMICAL JOURNAL | 1996年 / 319卷

关键词：

D O I：

10.1042/bj3190333

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：

Substrate isotope studies, solvent isotope studies, proton inventories and studies of V-max and K-m as a function of pH suggest an E(1)CB (V. E. Anderson (1991) in Enzyme Mechanisms for Isotope Effects (Cook, P. F., ed.), pp. 389-417, CRC Press, Boca Raton, FL) mechanism via an enolate intermediate for type II dehydroquinases involved in biosynthetic or catabolic pathways.

引用

页码：333 / 336

页数：4

共 20 条

[1]

ANDERSON VE, 1991, ENZYME MECH ISOTOPE, P389

[2]

CHAUDHURI S, 1991, BIOCHEM J, V275, P1

[3] PURIFICATION AND CHARACTERIZATION OF 3-DEHYDROQUINASE FROM ESCHERICHIA-COLI [J].