L-xylulose reductase
Enzyme
From Wikipedia, the free encyclopedia
Dicarbonyl/L-xylulose reductase, also known as carbonyl reductase II, is an enzyme that in human is encoded by the DCXR gene located on chromosome 17.
Structure
Function
DCSR catalyzes the reduction of several L-xylylose as well as a number of pentoses, tetroses, trioses, alpha-dicarbonyl compounds. The enzyme is involved in carbohydrate metabolism, glucose metabolism, the uronate cycle and may play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol.[2]
In enzymology, L-xylulose reductase (EC 1.1.1.10) is an enzyme that catalyzes the chemical reaction
Its two substrates are xylitol and the oxidised cofactor nicotinamide adenine dinucleotide phosphate (NADP+). The products are L-xylulose, reduced NADPH, and a proton.[3]
This enzyme belongs to the superfamily of short-chain 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:NADP+ 2-oxidoreductase (L-xylulose-forming).
Clinical significance
A deficiency is responsible for pentosuria. The insufficiency of L-xylulose reductase activity causes an inborn error of metabolism disease characterized by excessive urinary excretion of L-xylulose.
Over-expression and ectopic expression of the protein may be associated with prostate adenocarcinoma.[4]
