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

Authors
Journal
Tetrahedron
0040-4020
Publisher
Elsevier
Publication Date
Volume
54
Issue
52
Identifiers
DOI: 10.1016/s0040-4020(98)01005-9
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract 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.

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