L-Fuculokinase
Class of enzymes
L-Fuculokinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.1.51 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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L-Fuculokinase (EC 2.7.1.51) is an enzyme that catalyzes the chemical reaction
- ATP + L-fuculose (L-fuculokinase) ⇌ 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.
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phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor | |
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2.7.2: COOH acceptor | |
2.7.3: N acceptor | |
2.7.4: PO4 acceptor |
(P2O7)
(PO4-nucleoside)
Polymerase |
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Phosphorolytic 3' to 5' exoribonuclease | |||||
Nucleotidyltransferase | |||||
Guanylyltransferase | |||||
Other |
Phosphatidyltransferases | |
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Glycosyl-1-phosphotransferase |
(PO4; protein acceptor)
2.7.10: protein-tyrosine |
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2.7.11: protein-serine/threonine |
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2.7.12: protein-dual-specificity |
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2.7.13: protein-histidine |