EC 2 - Transferases
EC 2.7 - Transferring phosphorus-containing groups
EC 2.7.1 - Phosphotransferases with an alcohol group as acceptor
EC 2.7.1.26 - Riboflavin kinase
IntEnz Enzyme Nomenclature
EC 2.7.1.26
Names
flavokinase
riboflavin kinase (phosphorylating)
riboflavine kinase
RFK
Reaction
- ATP + riboflavin = ADP + FMN
Cofactor
Comments:
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preffering Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6].
Links to other databases
References
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The effect of the length of the side chain of flavins on reactivity with flavokinase.J. Biol. Chem. 240 : 1338-1340 (1965). [PMID: 14284745]
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Studies on plant flavokinase.Biochem. J. 70 : 66-71 (1958). [PMID: 13584303]
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The interaction of yeast flavokinase with riboflavin analogues.J. Biol. Chem. 194 : 747-754 (1952). [PMID: 14927668]
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Substrate specificity of liver flavokinase.Biochim. Biophys. Acta 65 : 326-332 (1962).
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An FMN hydrolase is fused to a riboflavin kinase homolog in plants.J. Biol. Chem. 280 : 38337-38345 (2005). [PMID: 16183635]
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Main physicochemical features of monofunctional flavokinase from Bacillus subtilis.Biochemistry (Moscow) 68 : 177-181 (2003). [PMID: 12693963]
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The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon.Microbiology 145 : 67-73 (1999). [PMID: 10206712]
[EC 2.7.1.26 created 1961, modified 2007]