L-Fuculokinase
| L-fuculokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.51 | ||||||||
| CAS number | 9026-64-6 | ||||||||
| 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 | ||||||||
| |||||||||
L-fuculokinase (EC 2.7.1.51) is an enzyme that catalyzes the chemical reaction
- ATP + L-fuculose
ADP + L-fuculose-1-phosphate
Thus, the two substrates of this enzyme are ATP and L-fuculose, whereas its two products are ADP and L-fuculose-1-phosphate.[1]
The gene name used for the gene that encodes L-fuculokinase is fucK.[2]
L-fuculokinase 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:L-fuculose 1-phosphotransferase. Other names in common use include L-fuculokinase (phosphorylating), and L-fuculose kinase. This enzyme participates in fructose and mannose metabolism.
References
- ↑ HEATH EC, GHALAMBOR MA (1962). "The metabolism of L-fucose. I. The purification and properties of L-fuculose kinase". J. Biol. Chem. 237: 2423–6. PMID 13905785.
- ↑ "NCBI gene database entry for E. coli O157:H7 fucK". National Center for Biotechnology Information. 2010-02-07. Retrieved 20 February 2010.