Fucokinase
| Fucokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.52 | ||||||||
| CAS no. | 37278-00-5 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Fucokinase (EC 2.7.1.52) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from pig liver and kidney converts β-L-fucose to β-L-fucose 1-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2][3] Fucokinase is the only enzyme that converts L-fucose to its 1-phosphate, which can be used to synthesize GDP-β-L-fucose, the donor substrate for all fucosyltransferases.[4] L-fucokinase activity can be detected in various tissues within an animal. For instance, rats and mice contain L-fucokinase widely distributed throughout tissues especially in the brain but the levels found vary widely among different species.[5]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:beta-L-fucose 1-phosphotransferase. Other names in common use include fucokinase (phosphorylating), fucose kinase, L-fucose kinase, L-fucokinase, ATP:6-deoxy-L-fucose 1-phosphotransferase, and ATP:L-fucose 1-phosphotransferase. Fucokinase is commonly abbreviated as fuc-K. The reaction is part of a salvage pathway for L-fucose.[6]
References
[edit]- ↑ Ishihara H, Massaro DJ, Heath EC (1968). "The metabolism of L-fucose. 3. The enzymatic synthesis of beta-L-fucose 1-phosphate". J. Biol. Chem. 243 (6): 1103–9. doi:10.1016/S0021-9258(19)56958-7. PMID 5646161.
- ↑ Butler W, Serif GS (1985). "Fucokinase, its anomeric specificity and mechanism of phosphate group transfer". Biochim. Biophys. Acta. 829 (2): 238–43. doi:10.1016/0167-4838(85)90193-1. PMID 2986701.
- ↑ Park SH, Pastuszak I, Drake R, Elbein AD (1998). "Purification to apparent homogeneity and properties of pig kidney L-fucose kinase". J. Biol. Chem. 273 (10): 5685–91. doi:10.1074/jbc.273.10.5685. PMID 9488699.
- ↑ Ng, Bobby G.; Rosenfeld, Jill A.; Emrick, Lisa; Jain, Mahim; Burrage, Lindsay C.; Lee, Brendan; Craigen, William J.; Bearden, David R.; Graham, Brett H.; Freeze, Hudson H. (6 December 2018). "Pathogenic Variants in Fucokinase Cause a Congenital Disorder of Glycosylation". American Journal of Human Genetics. 103 (6): 1030–1037. doi:10.1016/j.ajhg.2018.10.021. PMC 6288200. PMID 30503518.
- ↑ Honas, Bradley J.; Glassman, Urlene M.; Wiese, Thomas J. (2009). "Enzymatic Activity of α-L-Fucosidase and L-Fucokinase Across Vertebrate Animal Species". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 153 (4): 359–364. doi:10.1016/j.cbpb.2009.04.006. PMC 3413248. PMID 19394435.
- ↑ Enzyme 2.7.1.52 at KEGG Pathway Database.
