EC 1 - Oxidoreductases
EC 1.1 - Acting on the CH-OH group of donors
EC 1.1.1 - With NAD+ or NADP+ as acceptor
EC 1.1.1.271 - GDP-L-fucose synthase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.1.1.271
Names
Accepted name:
GDP-L-fucose synthase
Other
names:
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
GDP-fucose synthetase
GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
GDP-fucose synthetase
GDP-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Systematic name:
GDP-β-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Reaction
- GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-alpha-D-rhamnose + NADPH + H+
Comments:
Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Gene Ontology:
GO:0050577
References
-
An epimerase-reductase in L-fucose synthesis.J. Biol. Chem. 263 : 1693-1697 (1988). [PMID: 3338988]
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Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae.Glycobiology 10 : 1041-1047 (2000). [PMID: 11030750]
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Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli.J. Biol. Chem. 274 : 26743-26750 (1999). [PMID: 10480878]
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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 : 1601-1612 (1998). [PMID: 9862812]
[EC 1.1.1.271 created 2002, modified 2003]