2cfc

From Proteopedia

Revision as of 15:01, 30 October 2007

STRUCTURAL BASIS FOR STEREO SELECTIVITY IN THE (R)- AND (S)-HYDROXYPROPYLETHANE THIOSULFONATE DEHYDROGENASES

Overview

Epoxide metabolism in Xanthobacter autotrophicus Py2 results in the, conversion of epoxypropane to acetoacetate. Epoxide metabolism is, initiated by the nucleophilic addition of coenzyme M to the (R)- and, (S)-enantiomers of epoxypropane which forms the respective enantiomers of, 2-hydroxypropyl-coenyme M. The (R)- and (S)-enantiomers of 2-hydroxypropyl, coenzyme are oxidized to the achiral product 2-ketopropyl-CoM by two, stereoselective dehydrogenases. The dehydrogenases catalyzing these, reactions, termed (R)-hydroxypropyl-coenzyme M dehydrogenase (R-HPCDH) and, (S)-hydroxypropyl-coenzyme M dehydrogenase (S-HPCDH), are NAD(+)-dependent, enzymes belonging to the short chain dehydrogenase/reductase (SDR) family, of enzymes. In this study, the crystal structure of R-HPCDH cocrystallized, ... [(full description)]

About this Structure

2CFC is a [Single protein] structure of sequence from [Xanthobacter autotrophicus] with NAD and KPC as [ligands]. Active as [2-(R)-hydroxypropyl-CoM dehydrogenase], with EC number [1.1.1.268]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis for stereoselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases., Krishnakumar AM, Nocek BP, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jul 25;45(29):8831-40. PMID:16846226

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