D-xylose reductase (EC 1.1.1.307, XylR, XyrA, msXR, dsXR, monospecific xylose reductase, dual specific xylose reductase, NAD(P)H-dependent xylose reductase, xylose reductase) is an enzyme with systematic name xylitol:NAD(P)⁺ oxidoreductase.^[1]^[2]^[3]^[4]^[5]^[6]^[7]^[8] This enzyme catalyses the following chemical reaction

xylitol + NAD(P)⁺

\rightleftharpoons

D-xylose + NAD(P)H + H⁺

Xylose reductase catalyses the initial reaction in the xylose utilization pathway, the NAD(P)H dependent reduction of xylose to xylitol.

References[edit]

^ Neuhauser W, Haltrich D, Kulbe KD, Nidetzky B (September 1997). "NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme". The Biochemical Journal. 326 ( Pt 3) (Pt 3): 683–92. doi:10.1042/bj3260683. PMC 1218722. PMID 9307017.

^ Nidetzky B, Brüggler K, Kratzer R, Mayr P (December 2003). "Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies". Journal of Agricultural and Food Chemistry. 51 (27): 7930–5. doi:10.1021/jf034426j. PMID 14690376.

^ Iablochkova EN, Bolotnikova OI, Mikhaĭlova NP, Nemova NN, Ginak AI (2003). "[The activity of xylose reductase and xylitol dehydrogenase in yeasts]". Mikrobiologiia. 72 (4): 466–9. PMID 14526534.

^ Chen LC, Huang SC, Chuankhayan P, Chen CD, Huang YC, Jeyakanthan J, Pang HF, Men LC, Chen YC, Wang YK, Liu MY, Wu TK, Chen CJ (April 2009). "Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from Candida tropicalis". Acta Crystallographica Section F. 65 (Pt 4): 419–21. doi:10.1107/S1744309109008719. PMC 2664776. PMID 19342796.

^ Verduyn C, Van Kleef R, Frank J, Schreuder H, Van Dijken JP, Scheffers WA (March 1985). "Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis". The Biochemical Journal. 226 (3): 669–77. doi:10.1042/bj2260669. PMC 1144764. PMID 3921014.

^ Fernandes S, Tuohy MG, Murray PG (December 2009). "Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and heterologous expression of the native gene (Texr) and a double mutant (TexrK271R + N273D) with altered coenzyme specificity". Journal of Biosciences. 34 (6): 881–90. doi:10.1007/s12038-009-0102-7. PMID 20093741. S2CID 23211696.

^ Lee JK, Koo BS, Kim SY (October 2003). "Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis". Applied and Environmental Microbiology. 69 (10): 6179–88. Bibcode:2003ApEnM..69.6179L. doi:10.1128/AEM.69.10.6179-6188.2003. PMC 201247. PMID 14532079.

^ Woodyer R, Simurdiak M, van der Donk WA, Zhao H (March 2005). "Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa". Applied and Environmental Microbiology. 71 (3): 1642–7. Bibcode:2005ApEnM..71.1642W. doi:10.1128/AEM.71.3.1642-1647.2005. PMC 1065158. PMID 15746370.

External links[edit]

D-xylose+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase Alcohol oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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