GDP-L-fucose synthase

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.

References

• Chang S, Duerr B, Serif G (1988). "An epimerase-reductase in L-fucose synthesis". J. Biol. Chem. 263 (4): 1693–7. PMID 3338988. 
• 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 (10): 1041–7. doi:10.1093/glycob/10.10.1041. 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 (38): 26743–50. doi:10.1074/jbc.274.38.26743. 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 (12): 1601–12. doi:10.1016/S0969-2126(98)00157-9. PMID 9862812.