EC 2.7.1.26 - Riboflavin kinase

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IntEnz Enzyme Nomenclature
EC 2.7.1.26

Names

Accepted name:
riboflavin kinase
Other names:
FK
flavokinase
riboflavin kinase (phosphorylating)
riboflavine kinase
RFK
Systematic name:
ATP:riboflavin 5'-phosphotransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008531
CAS Registry Number: 9032-82-0
UniProtKB/Swiss-Prot: (40) [show] [UniProt]

References

  1. Chassy, B.M., Arsenis, C. and McCormick, D.B.
    The effect of the length of the side chain of flavins on reactivity with flavokinase.
    J. Biol. Chem. 240: 1338-1340 (1965). [PMID: 14284745]
  2. Giri, K.V., Krishnaswamy, P.R. and Rao, N.A.
    Studies on plant flavokinase.
    Biochem. J. 70: 66-71 (1958). [PMID: 13584303]
  3. Kearney, E.B.
    The interaction of yeast flavokinase with riboflavin analogues.
    J. Biol. Chem. 194: 747-754 (1952). [PMID: 14927668]
  4. McCormick, D.B. and Butler, R.C.
    Substrate specificity of liver flavokinase.
    Biochim. Biophys. Acta 65: 326-332 (1962).
  5. Sandoval, F.J. and Roje, S.
    An FMN hydrolase is fused to a riboflavin kinase homolog in plants.
    J. Biol. Chem. 280: 38337-38345 (2005). [PMID: 16183635]
  6. Solovieva, I.M., Tarasov, K.V. and Perumov, D.A.
    Main physicochemical features of monofunctional flavokinase from Bacillus subtilis.
    Biochemistry (Moscow) 68: 177-181 (2003). [PMID: 12693963]
  7. Solovieva, I.M., Kreneva, R.A., Leak, D.J. and Perumov, D.A.
    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]