IUBMB Enzyme Nomenclature

EC 1.1.1.271

Accepted name: GDP-L-fucose synthase

Reaction: GDP-β-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-α-D-mannose + NADPH + H+

For diagram click here.

Other name(s): GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase; GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)

Systematic name: GDP-β-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)

Comments: Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 113756-18-6

References:

1. Chang, S., Duerr, B. and Serif, G. An epimerase-reductase in L-fucose synthesis. J. Biol. Chem. 263 (1988) 1693-1697. [PMID: 3338988]

2. Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae. Glycobiology, 10, (2000) 1041-1047. [PMID: 11030750]

3. Menon, S., Stahl, M., Kumar, R., Xu, G.-Y. and Sullivan, F. Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli. J. Biol. Chem., 274, (1999) 26743-26750. [PMID: 10480878]

4. Somers, W.S., Stahl, M.L. and Sullivan, F.X. 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, (1998) 1601-1612. [PMID: 9862812]

[EC 1.1.1.271 created 2002, modified 2003]


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