Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases

Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases

Item
http://www.wikidata.org/entity/Q27641163
Computational design of Candida boidinii xylose reductase for altered cofactor specificityStructural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductaseAltering the coenzyme preference of xylose reductase to favor utilization of NADH enhances ethanol yield from xylose in a metabolically engineered strain of Saccharomyces cerevisiae.Increased ethanol productivity in xylose-utilizing Saccharomyces cerevisiae via a randomly mutagenized xylose reductase.Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.Genome sequence and physiological analysis of Yamadazyma laniorum f.a. sp. nov. and a reevaluation of the apocryphal xylose fermentation of its sister species, Candida tenuis.Altering coenzyme specificity of Pichia stipitis xylose reductase by the semi-rational approach CASTing.Multiple steps determine the overall rate of the reduction of 5alpha-dihydrotestosterone catalyzed by human type 3 3alpha-hydroxysteroid dehydrogenase: implications for the elimination of androgens.Genetic improvement of native xylose-fermenting yeasts for ethanol production.Point mutation of the xylose reductase (XR) gene reduces xylitol accumulation and increases citric acid production in Aspergillus carbonarius.Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies.Analysis and prediction of the physiological effects of altered coenzyme specificity in xylose reductase and xylitol dehydrogenase during xylose fermentation by Saccharomyces cerevisiae.The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida tenuis xylose reductase (AKR2B5) probed by site-directed mutagenesis and functional complementation studies.Obtaining partial purified xylose reductase from Candida guilliermondii.Fine tuning of coenzyme specificity in family 2 aldo-keto reductases revealed by crystal structures of the Lys-274-->Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+ and NADP+.Cloning, expression, and characterization of a novel xylose reductase from Rhizopus oryzae.
P2860

Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases

Item
http://www.wikidata.org/entity/Q27641163
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年論文
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2003年论文
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name
Structure of xylose reductase ...... family 2 aldo-keto reductases
@ast
Structure of xylose reductase ...... family 2 aldo-keto reductases
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Structure of xylose reductase ...... family 2 aldo-keto reductases
@nl
type
label
Structure of xylose reductase ...... family 2 aldo-keto reductases
@ast
Structure of xylose reductase ...... family 2 aldo-keto reductases
@en
Structure of xylose reductase ...... family 2 aldo-keto reductases
@nl
prefLabel
Structure of xylose reductase ...... family 2 aldo-keto reductases
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Structure of xylose reductase ...... family 2 aldo-keto reductases
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Structure of xylose reductase ...... family 2 aldo-keto reductases
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932
P356
P1433
P1476
Structure of xylose reductase ...... family 2 aldo-keto reductases
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932