2cfc
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2CFC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]] with NAD and KPC as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 2CFC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]] with NAD and KPC as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/2-(R)-hydroxypropyl-CoM_dehydrogenase 2-(R)-hydroxypropyl-CoM dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.268 1.1.1.268]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFC OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16846226 16846226] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16846226 16846226] | ||
| + | [[Category: 2-(R)-hydroxypropyl-CoM dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthobacter autotrophicus]] | [[Category: Xanthobacter autotrophicus]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:35:30 2007'' |
Revision as of 08:30, 30 October 2007
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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
Page seeded by OCA on Tue Oct 30 10:35:30 2007
