1m9h

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[[Image:1m9h.jpg|left|200px]]
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{{STRUCTURE_1m9h| PDB=1m9h | SCENE= }}
{{STRUCTURE_1m9h| PDB=1m9h | SCENE= }}
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'''Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor'''
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===Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor===
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==Overview==
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Corynebacterium 2,5-Diketo-D-gluconic acid reductase (2,5-DKGR) catalyzes the reduction of 2,5-diketo-D-gluconic acid (2,5-DKG) to 2-Keto-L-gulonic acid (2-KLG). 2-KLG is an immediate precursor to L-ascorbic acid (vitamin C), and 2,5-DKGR is, therefore, an important enzyme in a novel industrial method for the production of vitamin C. 2,5-DKGR, as with most other members of the aldo-keto reductase (AKR) superfamily, exhibits a preference for NADPH compared to NADH as a cofactor in the stereo-specific reduction of substrate. The application of 2,5-DKGR in the industrial production of vitamin C would be greatly enhanced if NADH could be efficiently utilized as a cofactor. A mutant form of 2,5-DKGR has previously been identified that exhibits two orders of magnitude higher activity with NADH in comparison to the wild-type enzyme, while retaining a high level of activity with NADPH. We report here an X-ray crystal structure of the holo form of this mutant in complex with NADH cofactor, as well as thermodynamic stability data. By comparing the results to our previously reported X-ray structure of the holo form of wild-type 2,5-DKGR in complex with NADPH, the structural basis of the differential NAD(P)H selectivity of wild-type and mutant 2,5-DKGR enzymes has been identified.
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{{ABSTRACT_PUBMED_14718658}}
==About this Structure==
==About this Structure==
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[[Category: Sanli, G.]]
[[Category: Sanli, G.]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:47:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:29:34 2008''

Revision as of 20:29, 2 July 2008

Image:1m9h.png

Template:STRUCTURE 1m9h

Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor

Template:ABSTRACT PUBMED 14718658

About this Structure

1M9H is a Single protein structure of sequence from Corynebacterium sp.. Full crystallographic information is available from OCA.

Reference

Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase., Sanli G, Banta S, Anderson S, Blaber M, Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. PMID:14718658

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