GDP-L-fucose synthase
From Wikipedia, the free encyclopedia
In enzymology, a GDP-L-fucose synthase (EC 1.1.1.271) is an enzyme that catalyzes the chemical reaction
- GDP-L-fucose + NADP+ GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+
Thus, the two substrates of this enzyme are GDP-L-fucose and NADP+, whereas its 3 products are GDP-4-dehydro-6-deoxy-D-mannose, 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 GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing). This enzyme is also called GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase. This enzyme participates in fructose and mannose metabolism.
[edit] References
- IUBMB entry for 1.1.1.271
- BRENDA references for 1.1.1.271 (Recommended.)
- PubMed references for 1.1.1.271
- PubMed Central references for 1.1.1.271
- Google Scholar references for 1.1.1.271
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- Mattila P, Rabina J, Hortling S, Helin J, Renkonen R (2000). "Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae". Glycobiology. 10: 1041–7. doi: . PMID 11030750.
- Menon S, Stahl M, Kumar R, Xu GY, Sullivan F (1999). "Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli". J. Biol. Chem. 274: 26743–50. doi: . PMID 10480878.
- Somers WS, Stahl ML, Sullivan FX (1998). "GDP-fucose synthetase from Escherichia coli: structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site". Structure. 6: 1601–12. doi: . PMID 9862812.