The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

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 of GDP-L-fucose and GDP-mannose biosynthesis, 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]
 
 


Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald