L-xylulose reductase
(Redirected from EC 1.1.1.10)
| DCXR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | DCXR, DCR, HCR2, HCRII, KIDCR, P34H, PNTSU, SDR20C1, XR, dicarbonyl/L-xylulose reductase, dicarbonyl and L-xylulose reductase | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 608347; MGI: 1915130; GeneCards: DCXR | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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| L-xylulose reductase | |||||||||
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 L-Xylulose reductase tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.10 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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
[edit]The DCXR gene encodes a membrane protein that is approximately 34 kDa in size and composed of 224 amino acids. The protein is highly expressed in the kidney and localizes to the cytoplasmic membrane.[5]
Function
[edit]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.[6]
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.[7]
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
[edit]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.[8]
See also
[edit]References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000169738 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039450 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Nakagawa J, Ishikura S, Asami J, Isaji T, Usami N, Hara A, Sakurai T, Tsuritani K, Oda K, Takahashi M, Yoshimoto M, Otsuka N, Kitamura K (2002). "Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney". J. Biol. Chem. 277 (20): 17883–91. doi:10.1074/jbc.M110703200. PMID 11882650.
- ↑ Zhao HT, Endo S, Ishikura S, Chung R, Hogg PJ, Hara A, El-Kabbani O (2009). "Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase". Cell. Mol. Life Sci. 66 (9): 1570–9. doi:10.1007/s00018-009-9065-y. PMC 11131457. PMID 19337691. S2CID 8332906.
- ↑ Enzyme 1.1.1.10 at KEGG Pathway Database.
- ↑ Cho-Vega JH, Tsavachidis S, Do KA, Nakagawa J, Medeiros LJ, McDonnell TJ (2007). "Dicarbonyl/L-xylulose reductase: a potential biomarker identified by laser-capture microdissection-micro serial analysis of gene expression of human prostate adenocarcinoma". Cancer Epidemiol. Biomarkers Prev. 16 (12): 2615–22. doi:10.1158/1055-9965.EPI-07-0684. PMID 18086765.
External links
[edit]- L-xylulose+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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