GDP-L-fucose synthase
| GDP-L-fucose synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.271 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a GDP-L-fucose synthase (EC 1.1.1.271) is an enzyme that catalyzes the chemical reaction
- GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+ GDP-L-fucose + NADP+
Thus, the three substrates of this enzyme are , NADPH, and H+, whereas its two products are and NADP+.
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.
Relevance in diseases[]
It has been reported that some cases of multiple sclerosis that present the HLA variant DRB3, present also autoimmunity against GDP-L-fucose synthase.[1][2] The same report points out that the autoimmune problem could derive from the gut microbiota.
See also[]
References[]
- ^ University of Zurich (2018, October 11). Link Between Gut Flora and Multiple Sclerosis Discovered. NeuroscienceNews. Retrieved October 11, 2018
- ^ R. Planas et al, GDP-l-fucose synthase is a CD4+ T cell–specific autoantigen in DRB3*02:02 patients with multiple sclerosis, Science Translational Medicine 10 Oct 2018, Vol. 10, Issue 462, eaat4301, DOI: 10.1126/scitranslmed.aat4301
- 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.
- EC 1.1.1
- NADPH-dependent enzymes
- Enzymes of unknown structure
- EC 1.1.1 stubs