fucokinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.1.52 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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In enzymology, a fucokinase (EC 2.7.1.52) is an enzyme that catalyzes the chemical reaction
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]
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