Biology:Fucokinase
In enzymology, a fucokinase (EC 2.7.1.52) is an enzyme that catalyzes the chemical reaction
- ATP + L-fucose [math]\displaystyle{ \rightleftharpoons }[/math] ADP + beta-L-fucose 1-phosphate
Thus, the two substrates of this enzyme are ATP and L-fucose, whereas its two products are ADP and beta-L-fucose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those 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. This enzyme participates in fructose and mannose metabolism. Fucokinase is the only enzyme that is converting L-fucose to fucose-1-phosphate and it can be further used for synthesizing GDP-fucose, which is the donor substrate for all fucosyltransferase. [1] L-Fucokinase activity can be detected in varied tissues within an animal. For instance, rats and mice contain L-fucokinase widely distributed throughout tissues especially higher in the brain. However, the levels of L-fucokinase in the brain is widely different among species.[2]
References
- ↑ Ng, Bobby G.; Rosenfeld, Jill A.; Emrick, Lisa; Jain, Mahim; Burrage, Lindsay C.; Lee, Brendan; Craigen, William J.; Bearden, David R. et al. (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. 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. PMID 19394435.
- "The metabolism of L-fucose. 3. The enzymatic synthesis of beta-L-fucose 1-phosphate". J. Biol. Chem. 243 (6): 1103–9. 1968. PMID 5646161.
- "Fucokinase, its anomeric specificity and mechanism of phosphate group transfer". Biochim. Biophys. Acta 829 (2): 238–43. 1985. doi:10.1016/0167-4838(85)90193-1. PMID 2986701.
- "Purification to apparent homogeneity and properties of pig kidney L-fucose kinase". J. Biol. Chem. 273 (10): 5685–91. 1998. doi:10.1074/jbc.273.10.5685. PMID 9488699.
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