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Riboflavin kinase

riboflavin kinase, flavokinase, RFK
Riboflavin kinase (RFK; EC 2.7.1.26) is an essential enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN), an obligatory step in vitamin B2 utilization and flavin cofactor synthesis (Karthikeyan et al., 2003 [PubMed 12623014]).[supplied by OMIM, Nov 2009] (from NCBI)
Top mentioned proteins: Presenilin-1, ACID, CAN, STEP, HAD
Papers on riboflavin kinase
Structural insights into the synthesis of FMN in prokaryotic organisms.
New
Medina et al., Zaragoza, Spain. In Acta Crystallogr D Biol Crystallogr, Jan 2016
The RFK module of FADS is a homologue of eukaryotic monofunctional RFKs, while the FMNAT module lacks homologyto eukaryotic enzymes involved in FAD production.
Quaternary organization in a bifunctional prokaryotic FAD synthetase: Involvement of an arginine at its adenylyltransferase module on the riboflavin kinase activity.
New
Medina et al., Zaragoza, Spain. In Biochim Biophys Acta, Aug 2015
Prokaryotic FAD synthetases (FADSs) are bifunctional enzymes composed of two modules, the C-terminal module with ATP:riboflavin kinase (RFK) activity, and the N-terminus with ATP:FMN adenylyltransferase (FMNAT) activity.
Identification of riboflavin: revealing different metabolic characteristics between Escherichia coli BL21(DE3) and MG1655.
New
Qi et al., Jinan, China. In Fems Microbiol Lett, Jun 2015
Comparing the enzyme sequences involved in riboflavin metabolism between BL21 and MG1655, we identified a site mutation on the 115 residue of bifunctional riboflavin kinase/FMN adenylyltransferase (RibF) in BL21.
Identification of differentially expressed genes associated with flower color in peach using genome-wide transcriptional analysis.
Gao et al., Nanjing, China. In Genet Mol Res, 2014
The results suggest that hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase, 2-oxoglutarate-dependent dioxygenase, isoflavone reductase, riboflavin kinase, zeta-carotene desaturase, and ATP binding cassette transporter may be associated with the flower color formation.
Exploring the role of sigma factor gene expression on production by Corynebacterium glutamicum: sigma factor H and FMN as example.
Wendisch et al., Bielefeld, Germany. In Front Microbiol, 2014
To test if sigH overexpression can be exploited for production of riboflavin-derived FMN or FAD, the endogenous gene for bifunctional riboflavin kinase/FMN adenyltransferase was co-expressed with sigH from a plasmid.
Riboflavin (vitamin B2 ) deficiency impairs NADPH oxidase 2 (Nox2) priming and defense against Listeria monocytogenes.
Krönke et al., Köln, Germany. In Eur J Immunol, 2014
Riboflavin, also known as vitamin B2 , is converted by riboflavin kinase (RFK) into flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential cofactors of dehydrogenases, reductases, and oxidases including the phagocytic NADPH oxidase 2 (Nox2).
Antitrypanosomal activity & docking studies of components of Crateva adansonii DC leaves: novel multifunctional scaffolds.
Gray et al., New Delhi, India. In Curr Top Med Chem, 2013
Their affinity towards the receptor sites of trypanothione reductase, riboflavin kinase, rohedsain, glutathione synthetase & sterol-14α-demethylase (CYP51) of Trypanosoma brucei were evaluated according to the resulting docking energies.
Antitrypanosomal activity & docking studies of isolated constituents from the lichen Cetraria islandica: possibly multifunctional scaffolds.
Singla et al., New Delhi, India. In Curr Top Med Chem, 2013
Docking studies (GRIP technique) of these molecules revealed their strong affinity towards possible targets of Trypanosoma brucei such as riboflavin kinase, sterol-14α-demethylase (CYP51), rohedsain and glutathione synthetase.
Metabolic engineering of Escherichia coli for the production of riboflavin.
Zhao et al., In Microb Cell Fact, 2013
By further modulating the expression of ribF (encodes riboflavin kinase) for reducing the conversion of riboflavin to FMN in RF05S, the final engineering strain RF05S-M40 could produce 1036.1 mg/L riboflavin in LB medium at 37°C.
Flavoproteins are potential targets for the antibiotic roseoflavin in Escherichia coli.
Mack et al., Mannheim, Germany. In J Bacteriol, 2013
Roseoflavin is converted to the flavin mononucleotide (FMN) analog roseoflavin mononucleotide (RoFMN) by flavokinase and to the flavin adenine dinucleotide (FAD) analog roseoflavin adenine dinucleotide (RoFAD) by FAD synthetase.
The flavoenzyme azobenzene reductase AzoR from Escherichia coli binds roseoflavin mononucleotide (RoFMN) with high affinity and is less active in its RoFMN form.
Mack et al., Mannheim, Germany. In Biochemistry, 2013
Roseoflavin is a structural riboflavin analogue and is converted to the flavin mononucleotide (FMN) analogue roseoflavin mononucleotide (RoFMN) by flavokinase.
The prokaryotic FAD synthetase family: a potential drug target.
Review
Medina et al., Zaragoza, Spain. In Curr Pharm Des, 2012
The first step before searching for selective inhibitors of FADS is to understand the structural and functional mechanisms for the riboflavin kinase and FMN adenylyltransferase activities of the prokaryotic enzyme, and particularly to identify their differential functional characteristics with regard to the enzymes performing similar functions in other organisms, particularly humans.
Death receptors 4 and 5 activate Nox1 NADPH oxidase through riboflavin kinase to induce reactive oxygen species-mediated apoptotic cell death.
GeneRIF
Kim et al., Suwŏn, South Korea. In J Biol Chem, 2012
DR4 and DR5 have a capability to activate Nox1 by recruiting RFK, resulting in ROS-mediated apoptotic cell death in tumor cells.
Role of key residues at the flavin mononucleotide (FMN):adenylyltransferase catalytic site of the bifunctional riboflavin kinase/flavin adenine dinucleotide (FAD) Synthetase from Corynebacterium ammoniagenes.
Medina et al., Zaragoza, Spain. In Int J Mol Sci, 2011
In mammals and in yeast the conversion of Riboflavin (RF) into flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) is catalysed by the sequential action of two enzymes: an ATP:riboflavin kinase (RFK) and an ATP:FMN adenylyltransferase (FMNAT).
Involvement of riboflavin kinase expression in cellular sensitivity against cisplatin.
GeneRIF
Kohno et al., Kitakyūshū, Japan. In Int J Oncol, 2011
levels of riboflavin kinase expression correlate well with Gleason score, known as a good indicator of patient prognosis
Riboflavin kinase couples TNF receptor 1 to NADPH oxidase.
Impact
GeneRIF
Krönke et al., Köln, Germany. In Nature, 2009
results suggest that TNF, through the activation of RFK, enhances the incorporation of FAD in NADPH oxidase enzymes, a critical step for the assembly and activation of NADPH oxidase
Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.
GeneRIF
Zhang et al., Dallas, United States. In Biochemistry, 2003
the structure of riboflavin kinase cocrystallized with both MgADP and FMN is reported; drastic conformational changes associated with flavin binding are observed primarily at the so-called Flap I and Flap II loop regions
Three biotechnical processes using Ashbya gossypii, Candida famata, or Bacillus subtilis compete with chemical riboflavin production.
Review
Seulberger et al., Jülich, Germany. In Appl Microbiol Biotechnol, 2000
To obtain riboflavin production with the gram-positive bacterium Bacillus subtilis requires at least the deregulation of purine synthesis and a mutation in a flavokinase/FAD-synthetase.
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