IntEnz

EC 2.7.1.26 - Riboflavin kinase

IntEnz Enzyme Nomenclature
EC 2.7.1.26

Names

Reaction

• 14357 [IUBMB]
  ATP

  ATP

  Name origin: UniProt - CHECKED (C)

  CHEBI:30616

  Formula: C10H12N5O13P3
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  riboflavin

  riboflavin

  Name origin: UniProt - CHECKED (C)

  CHEBI:57986

  Formula: C17H19N4O6
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  ADP

  ADP

  Name origin: UniProt - CHECKED (C)

  CHEBI:456216

  Formula: C10H12N5O10P2
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  FMN

  FMN

  Name origin: UniProt - CHECKED (C)

  CHEBI:58210

  Formula: C17H18N4O9P
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Mg²⁺ or Zn²⁺ or Mn²⁺

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

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]