D-xylulose reductase

D-xylulose reductase
D-xylulose reductase homotetramer, Gluconobacter oxydans
Identifiers
EC no.	1.1.1.9
CAS no.	9028-16-4
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that catalyzes the chemical reaction

xylitol + NAD⁺ ${\displaystyle \rightleftharpoons }$ D-xylulose + NADH + H⁺

Thus, the two substrates of this enzyme are xylitol and NAD⁺, whereas its 3 products are D-xylulose, NADH, 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 xylitol:NAD⁺ 2-oxidoreductase (D-xylulose-forming). Other names in common use include NAD⁺-dependent xylitol dehydrogenase, xylitol dehydrogenase, erythritol dehydrogenase, 2,3-cis-polyol(DPN) dehydrogenase (C3-5), pentitol-DPN dehydrogenase, and xylitol-2-dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.

Structural studies[]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1ZEM.

References[]

• Chiang C, Knight SG (1960). "A new pathway of pentose metabolism". Biochem. Biophys. Res. Commun. 3 (5): 554–9. doi:10.1016/0006-291X(60)90174-1. PMID 13692998.
• Hickman J; Ashwell G (1959). "A sensitive and stereospecific enzymatic assay for xylulose". J. Biol. Chem. 234: 758–761. PMID 13654257.
• Jakoby WB, Fredericks J (1961). "Erythritol dehydrogenase from Aerobacter aerogenes". Biochim. Biophys. Acta. 48: 26–32. doi:10.1016/0006-3002(61)90511-X. PMID 13789254.