The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RFK  -  riboflavin kinase

Homo sapiens

Synonyms: ATP:riboflavin 5'-phosphotransferase, FLJ11149, Flavokinase, RIFK, Riboflavin kinase
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of RFK


High impact information on RFK

  • Consistent patterns of sequence similarities have identified the open reading frame of unknown function YDR236c as a candidate to encode flavokinase in Saccharomyces cerevisiae [4].
  • The structures of the flavin-bound RFK obtained by soaking pre-existing crystals were also reported [5].
  • Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B(2)) in the presence of ATP and Mg(2+) to form the active cofactor FMN, which can be further converted to FAD [5].
  • These structures revealed that RFK adopts a novel kinase fold and utilizes a unique nucleotide binding site [5].
  • Flavokinase was purified, for the first time from a plant source [mung bean (Phaseolus aureus)] by affinity chromatography in the presence of orthophosphate and by using C-8 ATP-agarose (ATP linked through the C-8 position to beaded agarose), Cibacron Blue and riboflavin--Sepharoses [6].

Biological context of RFK


Anatomical context of RFK

  • 1. Flavokinase isolated from 18-day chick embryo liver shows optimal activity at pH 8.6, in the presence of the divalent cations Zn2+, Ca2+ and Mn2+ [7].

Associations of RFK with chemical compounds

  • The structure of human RFK revealed a six-stranded antiparallel beta barrel core structurally similar to the riboflavin synthase/ferredoxin reductase FAD binding domain fold [8].
  • Plant flavokinase. Affinity-chromatographic procedure for the purification of the enzyme from mung-bean (Phaseolus aureus) seeds and conformational changes on its interaction with orthophosphate [6].
  • Flavin adenine dinucleotide synthetase, separable from flavokinase in mammals, prefers Mg2+ [9].
  • The antinociceptive effect was not inhibited by the pretreatment with cadmium sulfate (1 mg/kg), an inhibitor of flavokinase [10].


  1. Chemical and enzymatic properties of riboflavin analogues. Walsh, C., Fisher, J., Spencer, R., Graham, D.W., Ashton, W.T., Brown, J.E., Brown, R.D., Rogers, E.F. Biochemistry (1978) [Pubmed]
  2. Continuous fluorescence assay, partial purification and properties of flavokinase from Megasphaera elsdenii. Mayhew, S.G., Wassink, J.H. Meth. Enzymol. (1980) [Pubmed]
  3. A continuous fluorometric assay for flavokinase. Properties of flavokinase from Peptostreptococcus elsdenii. Mayhew, S.G., Wassink, J.H. Biochim. Biophys. Acta (1977) [Pubmed]
  4. Molecular characterization of FMN1, the structural gene for the monofunctional flavokinase of Saccharomyces cerevisiae. Santos, M.A., Jimenez, A., Revuelta, J.L. J. Biol. Chem. (2000) [Pubmed]
  5. Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. Karthikeyan, S., Zhou, Q., Osterman, A.L., Zhang, H. Biochemistry (2003) [Pubmed]
  6. Plant flavokinase. Affinity-chromatographic procedure for the purification of the enzyme from mung-bean (Phaseolus aureus) seeds and conformational changes on its interaction with orthophosphate. Sobhanaditya, J., Rao, N.A. Biochem. J. (1981) [Pubmed]
  7. The effect of riboflavin binding protein (RPB) on flavokinase catalytic activity. Słomczynska, M., Zak, Z. Comp. Biochem. Physiol., B (1987) [Pubmed]
  8. Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch. Karthikeyan, S., Zhou, Q., Mseeh, F., Grishin, N.V., Osterman, A.L., Zhang, H. Structure (Camb.) (2003) [Pubmed]
  9. A trail of research on cofactors: an odyssey with friends. McCormick, D.B. J. Nutr. (2000) [Pubmed]
  10. Characterization of the antinociceptive and anti-inflammatory activities of riboflavin in different experimental models. Bertollo, C.M., Oliveira, A.C., Rocha, L.T., Costa, K.A., Nascimento, E.B., Coelho, M.M. Eur. J. Pharmacol. (2006) [Pubmed]
WikiGenes - Universities