ExplorEnz: EC 2.7.1.26

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2.7.1.26

Accepted name:

riboflavin kinase

Reaction:

ATP + riboflavin = ADP + FMN

For diagram of FAD biosynthesis, click here

Other name(s):

flavokinase; FK; RFK

Systematic name:

ATP:riboflavin 5′-phosphotransferase

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 preferring 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:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-82-0

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 (1965) 1338–1340. [PMID: 14284745]
2.	Giri, K.V., Krishnaswamy, P.R. and Rao, N.A. Studies on plant flavokinase. Biochem. J. 70 (1958) 66–71. [PMID: 13584303]
3.	Kearney, E.B. The interaction of yeast flavokinase with riboflavin analogues. J. Biol. Chem. 194 (1952) 747–754. [PMID: 14927668]
4.	McCormick, D.B. and Butler, R.C. Substrate specificity of liver flavokinase. Biochim. Biophys. Acta 65 (1962) 326–332.
5.	Sandoval, F.J. and Roje, S. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 280 (2005) 38337–38345. [DOI] [PMID: 16183635]
6.	Solovieva, I.M., Tarasov, K.V. and Perumov, D.A. Main physicochemical features of monofunctional flavokinase from Bacillus subtilis. Biochemistry (Mosc.) 68 (2003) 177–181. [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 (1999) 67–73. [DOI] [PMID: 10206712]

[EC 2.7.1.26 created 1961, modified 2007]