L-Fuculokinase
| L-Fuculokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.51 | ||||||||
| CAS no. | 9026-64-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
L-Fuculokinase (EC 2.7.1.51) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from Escherichia coli converts the deoxy sugar, L-fuculose, to L-fuculose 1-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1] The gene name used for the gene that encodes L-fuculokinase is fucK.[2]
L-Fuculokinase is a transferase, specifically one 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.[3]
References
- ↑ Heath EC, Ghalambor MA (1962). "The metabolism of L-fucose. I. The purification and properties of L-fuculose kinase". J. Biol. Chem. 237 (8): 2423–6. doi:10.1016/S0021-9258(19)73767-3. PMID 13905785.
- ↑ "NCBI gene database entry for E. coli O157:H7 fucK". National Center for Biotechnology Information. 2010-02-07. Retrieved 20 February 2010.
- ↑ Enzyme 2.7.1.51 at KEGG Pathway Database.
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