Riboflavin kinase

From Wikipedia, the free encyclopedia

In enzymology, a riboflavin kinase (EC 2.7.1.26) is an enzyme that catalyzes the chemical reaction

ATP + riboflavin $\rightleftharpoons$ ADP + FMN

Thus, the two substrates of this enzyme are ATP and riboflavin, whereas its two products are ADP and FMN.

This enzyme 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:riboflavin 5'-phosphotransferase. This enzyme is also called flavokinase. This enzyme participates in riboflavin metabolism. However, archaeal riboflavin kinases are supposedly generally utilizing CTP rather than ATP as the donor nucleotide.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1N05, 1N06, 1N07, 1N08, 1NB0, 1NB9, 1P4M, 1Q9S, 2P3M, 2VBS, 2VBT, 2VBU and 2VBV.

[edit] References

IUBMB entry for 2.7.1.26
BRENDA references for 2.7.1.26 (Recommended.)
PubMed references for 2.7.1.26
PubMed Central references for 2.7.1.26
Google Scholar references for 2.7.1.26
CHASSY BM, ARSENIS C, MCCORMICK DB (1965). "THE EFFECT OF THE LENGTH OF THE SIDE CHAIN OF FLAVINS ON REACTIVITY WITH FLAVOKINASE". J. Biol. Chem. 240: 1338–40. PMID 14284745.
GIRI KV, KRISHNASWAMY PR, RAO NA (1958). "Studies on plant flavokinase". Biochem. J. 70: 66–71. PMID 13584303.
KEARNEY EB (1952). "The interaction of yeast flavokinase with riboflavin analogues". J. Biol. Chem. 194: 747–54. PMID 14927668.
McCormick DB and Butler RC (1962). "Substrate specificity of liver flavokinase". Biochim. Biophys. Acta 65: 326–332.
Sandoval FJ, Roje S (2005). "An FMN hydrolase is fused to a riboflavin kinase homolog in plants". J. Biol. Chem. 280: 38337–45. PMID 16183635.
Solovieva IM, Tarasov KV, Perumov DA (Mosc). "Main physicochemical features of monofunctional flavokinase from Bacillus subtilis". B Biochemistry.: 177–81. PMID 12693963.
Solovieva IM, Kreneva RA, Leak DJ, Perumov DA (Pt 1). "The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon". Microbiology. 145: 67–73. PMID 10206712.
Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M (2007). "A CTP-Dependent Archaeal Riboflavin Kinase Forms a Bridge in the Evolution of Cradle-Loop Barrels.". Structure. 12: 1577–90. PMID 18073108.