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

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 + pro...

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Bibliographic Details
Published in:	Tetrahedron Vol. 54; no. 52; pp. 15975 - 15982
Main Authors:	Hallis, Tina M., Liu, Hung-wen
Format:	Journal Article
Language:	English
Published:	Elsevier Ltd 24-12-1998
Online Access:	Get full text
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Summary:	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. 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 step for (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.
ISSN:	0040-4020 1464-5416
DOI:	10.1016/S0040-4020(98)01005-9