Main Physicochemical Features of Monofunctional Flavokinase from Bacillus subtilis

  title={Main Physicochemical Features of Monofunctional Flavokinase from Bacillus subtilis},
  author={Irina M Solovieva and K. V. Tarasov and Daniel A. Perumov},
  journal={Biochemistry (Moscow)},
The main properties of a monofunctional riboflavin kinase from B. subtilis have been studied for the first time; the enzyme is responsible for a key reaction in flavin biosynthesis—the ATP-dependent phosphorylation of riboflavin with production of flavin mononucleotide. The active form of the enzyme is a monomer with molecular weight of about 26 kD with a strict specificity for reduced riboflavin. To display its maximum activity, the enzyme needs ATP and Mg2+. During the phosphorylation of… 

Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes

This work focuses on regulation of the FMN synthesis in Corynebacterium ammoniagenes by the inhibition of its RFK activity by substrates and products of the reaction.

The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status

The dependence of FMN synthesis rate on riboflavin concentration shows saturation kinetics with a sigmoidal shape, and newly synthesized FAD can be exported from intact mitochondria via a putative FAD exporter.

Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo‐flavoproteins

The data indicate that FAD release may represent the rate‐limiting step of the whole catalytic cycle and that the process leading to FAD synthesis, and delivery to client apoproteins may be tightly controlled.

Mitochondrial localization of human FAD synthetase isoform 1.

Human riboflavin kinase: Species‐specific traits in the biosynthesis of the FMN cofactor

Observations support HsRFK as potential therapeutic target because of its key functions, while also envisage bacterial RFK modules as potential antimicrobial targets.

Multifunctional regulatory mutation in Bacillus subtilis flavinogenesis system

Genetic and biochemical analysis showed that the ribU1 mutation determines a trans-acting factor that simultaneously regulates activity of riboflavin and truB-ribC-rpsO operons.

Investigation of recombinant protein production by Escherichia coli : expression of Green fluorescent protein and a co-factor dependent flavinated enzyme

This thesis summarises work done on the Escherichia coli strain MG1655 expressing a Green Fluorescent Protein and the flavo-protein N-methyl-L-tryptophan oxidase (MTOX) product and examines the effect foreign protein production has on cell growth parameters, comparable to that seen in E.coli fermentations.



Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins.

The two enzymatic activities, flavokinase and FADH2 pyrophosphorylase, although not separated during the purification procedure, are distinguished by differences in metal ion specificity, in concentration dependence for ATP, and in the inhibitory effects of riboflavin analogues.

Regulation of Riboflavin Biosynthesis inBacillus subtilis Is Affected by the Activity of the Flavokinase/Flavin Adenine Dinucleotide Synthetase Encoded byribC

It is shown that the ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities, which indicates that flavin nucleotides, but not riboflavin, have an effector function for regulation of rib oflavin biosynthesis in B. subtilis.

Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production

The cloning of a bifunctional FAD synthetase gene, which shows flavokinase and FMN adenylyltransferase activities, from Corynebacterium ammoniagenes was tried by hybridization with synthetic DNAs

The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon.

Measurement of flavokin enzyme activity in cell extracts demonstrated that ribR encodes a monofunctional flavokinase which converts rib oflavin into FMN but not to FAD, and is specific for the reduced form of riboflavin.

Functional organization of the riboflavin biosynthesis operon from Bacillus subtilis SHgw

The data presented argue against regulation by attenuation of riboflavin biosynthesis genes within the Bacillus subtilis SHgw chromosome.

[Analgos of riboflavin, lumiflavin and alloxazine derivatives. II. Effect of roseoflavin on 6,7-dimethyl-8-ribityllumazine and riboflavin synthetase synthesis and growth of Bacillus subtilis].

Effect of rozeoflavin and other rib oflavin analogues on the growth and regulatory characteristics of Bacillus subtilis strains with different genetic state of riboflav in operon is studied.

[Cloning of ribR, an additional regulatory gene of the Bacillus subtilis riboflavin operon].

A 13.0-kb EcoRI fragment of Bacillus subtilis DNA carrying an additional regulatory ribR gene of riboflavin operon was cloned on the basis of resistance to 7, 8-dimethyl-10

Genetic mapping of regulatory mutations ofBacillus subtilis riboflavin operon

Seven mutations leading to riboflavin overproduction in Bacillus subtilis were found to be linked to the markerdnaF133 by transformation, and results of transduction and transformation crosses suggest the following order of markers.