Disease relevance of RFK

• Nearly all of the analogues that possess D-ribityl groups are found to be processed to the FAD level by the flavokinase/FAD synthetase system of Brevibacterium ammoniagenes [1].
• Continuous fluorescence assay, partial purification and properties of flavokinase from Megasphaera elsdenii [2].
• Use of this assay is illustrated in a procedure for the partial purification of flavokinase from the strict anaerobe Peptostreptococcus elsdenii [3].

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

• The effect of riboflavin binding protein (RPB) on flavokinase catalytic activity [7].

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].

References