1m9h

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spinqualitylabelsall models 1m9h, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1M9H is a Single protein structure of sequence from Corynebacterium sp. with SO4 and NAD as ligands. 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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