Fucokinase
| fucokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.52 | ||||||||
| CAS number | 37278-00-5 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
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
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-galactose 1-phosphotransferase, and ATP:L-fucose 1-phosphotransferase. Fucokinase is commonly abbreviated as fuc-K. This enzyme participates in fructose and mannose metabolism.
References
- 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. 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.