NDLI: Substrate binding to Candida tenuis xylose reductase during catalysis

Content Provider	Royal Society of Chemistry (RSC)
Author	Vogl, Michael Brecker, Lothar
Copyright Year	2013
Abstract	Candida tenuis xylose reductase (CtXR) is studied by in situ NMR, saturation transfer difference (STD) NMR, and molecular docking with respect to its substrate and coenzyme binding in ternary complexes. The natural substrate Xyl as well as Glc and methyl-glucosides preferentially bind as α-anomers of the pyranose forms. These α-anomers are transformed faster, predominately leading to STD effects in the formed products, and can be better docked into the CtXR active site than the β-anomer. The reduction is initiated by α-Xylp ring opening prior to hydride transfer from NADH. Binding and transformation of unnatural 2,4-dichloroacetophenone is not as good, although it is reduced with very high catalytic efficiency. STD NMR indicates a reasonable amount to leave the ternary complex in unreduced form. The molecular docking calculation confirms this result, as only a couple of the investigated ternary complexes allow reduction of the substrates.
Starting Page	25997
Ending Page	26004
Page Count	8
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	3
Issue Number	48
Journal	RSC Advances
DOI	10.1039/c3ra41448e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Candida albicans Active site Docking (molecular) Cofactor (biochemistry) Pyranose Tenuis consonant Xylose NADH Candida Nicotinamide adenine dinucleotide Hydride Nuclear magnetic resonance Glc
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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