D-xylose 1-dehydrogenase (NADP+)

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In enzymology, a D-xylose 1-dehydrogenase (NADP+) (EC 1.1.1.179) is an enzyme that catalyzes the chemical reaction

D-xylose + NADP⁺ $\rightleftharpoons$ D-xylono-1,5-lactone + NADPH + H⁺

Thus, the two substrates of this enzyme are D-xylose and NADP⁺, whereas its 3 products are D-xylono-1,5-lactone, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-xylose:NADP+ 1-oxidoreductase. Other names in common use include D-xylose (nicotinamide adenine dinucleotide phosphate), dehydrogenase, D-xylose-NADP+ dehydrogenase, D-xylose:NADP+ oxidoreductase, and D-xylose 1-dehydrogenase (NADP+).

[edit] References

IUBMB entry for 1.1.1.179
BRENDA references for 1.1.1.179 (Recommended.)
PubMed references for 1.1.1.179
PubMed Central references for 1.1.1.179
Google Scholar references for 1.1.1.179
Wissler JH (1977). "D-Xylose:NADP oxidoreductase of arterial vessels and eye lens: a new enzyme and a final link in ATP-independent cycling of reducing eqivalents in aldose-polyol-ketose interconversion". Hoppe-Seyler's Z. Physiol. Chem. 358: 1300–1301.
Wissler JH (1978). "Direct spectrophotometric and specific quantitative determination of free and bound D-xylose by analytical application of a new enzyme, D-xylose:NADP-oxidoreductase". Fresenius' Z. Anal. Chem. 290: 179–180. doi:10.1007/BF00482334.