Fucokinase

In enzymology, a fucokinase (EC 2.7.1.52) is an enzyme that catalyzes the chemical reaction

ATP + L-fucose ADP + beta-L-fucose 1-phosphate
fucokinase
Identifiers
EC number2.7.1.52
CAS number37278-00-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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
  1. 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.
  2. 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.


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