D-xylose 1-dehydrogenase (NADP+)
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| D-xylose 1-dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.179 | ||||||||
| CAS no. | 83534-37-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a D-xylose 1-dehydrogenase (NADP+) (EC 1.1.1.179) is an enzyme that catalyzes the chemical reaction
- D-xylose + NADP+ 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+).
References
- 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 equivalents 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 (2): 179–180. doi:10.1007/BF00482334. S2CID 83089543.
