Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/1887
Title: Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase
Authors: Şanlı Mohamed, Gülşah
Banta, Scott
Anderson, Stephen
Blaber, Michael
Şanlı Mohamed, Gülşah
Keywords: Corynebacterium
Aldo keto reductase
Ascorbic acid
Enzyme engineering
Vitamin C
Issue Date: Feb-2004
Publisher: John Wiley and Sons Inc.
Source: Şanlı Mohamed, G., Banta, S., Anderson, S., and Blaber, M. (2004). Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Science, 13(2), 504-512. doi:10.1110/ps.03450704
Abstract: Carynebacterium 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.
URI: http://doi.org/10.1110/ps.03450704
http://hdl.handle.net/11147/1887
ISSN: 0961-8368
0961-8368
1469-896X
Appears in Collections:Chemistry / Kimya
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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