Stereospecificity of hydride transfer for the catalytically recycled NAD+ in CDP-D-glucose 4,6-dehydratase

被引：8

作者：

Hallis, TM ^{[1
]}

Liu, HW ^{[1
]}

机构：

[1] Univ Minnesota, Dept Chem, Minneapolis, MN 55455 USA

来源：

TETRAHEDRON | 1998年 / 54卷 / 52期

关键词：

D O I：

10.1016/S0040-4020(98)01005-9

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

CDP-D-glucose 4,6-dehydratase (E-od), found in the biosynthetic pathway of 3,6-dideoxysugars, contains a tightly bound NAD(+) that is recycled during catalysis. The stereochemical preference of the hydride transfer to and from the coenzyme in E-od was determined to be pro-S by analyzing the NAD(+) produced when the apoenzyme was incubated with stereospecifically labeled NADH and its product, CDP-6-deoxy-D-glycero-L-threo-4-hexulose (C) 1998 Elsevier Science Ltd. All rights reserved.

引用

页码：15975 / 15982

页数：8

共 20 条

[1]

Arnold L J Jr, 1978, Methods Enzymol, V54, P223

[2] STEREOSPECIFICITY OF L-MYO-INOSITOL-1-PHOSPHATE SYNTHASE FOR NICOTINAMIDE ADENINE-DINUCLEOTIDE [J].