Information on EC 2.7.1.26 - riboflavin kinase:
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EC NUMBERCOMMENTARY
2.7.1.26-

RECOMMENDED NAMEGeneOntology No.
riboflavin kinaseGO:0008531

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + riboflavin = ADP + FMN
show the reaction diagram		----
ATP + riboflavin = ADP + FMN
show the reaction diagram		ordered bi bi mechanism in which riboflavin binds first followed by ATP. ADP is released first followed by FMNRattus norvegicus-641239
ATP + riboflavin = ADP + FMN
show the reaction diagram		ordered reaction mechanism, FMN binding o the binary enzyme-MgADP complex induces important conformational changesHomo sapiens-657963

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phospho group transfer----

PATHWAYKEGG LinkMetaCyc Link
5,6-dimethylbenzimidazole biosynthesis-PWY-5523
flavin biosynthesis I (bacteria and plants)-RIBOSYN2-PWY
flavin biosynthesis III (fungi)-PWY-6168
flavin biosynthesis IV (mammalian)-PWY66-366

SYSTEMATIC NAMEIUBMB Comments
ATP:riboflavin 5'-phosphotransferaseThe cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
AtFMN/FHyArabidopsis thaliana-bifunctional enzyme has riboflavin kinase and FMN hydrolase activities680633
FK----
flavokinase----
flavokinaseHomo sapiens, Mus musculus--705886
flavokinase/FAD synthetaseBacillus subtilis--687408
flavokinase/FAD synthetaseStreptomyces davawensisA3FM23-687408
flavokinase/flavin adenine dinucleotide synthetaseBacillus subtilis-bifunctional enzyme EC 2.7.1.26/EC 2.7.2.2687408
flavokinase/flavin adenine dinucleotide synthetaseStreptomyces davawensisA3FM23bifunctional enzyme EC 2.7.1.26/EC 2.7.2.2687408
kinase, riboflavin----
RFKHomo sapiens--657963
RibCBacillus subtilis--687408
RibCStreptomyces davawensisA3FM23-687408
riboflavin kinaseNicotiana tabacum--703642
riboflavin kinaseHomo sapiens, Mus musculus--705886
riboflavine kinase----
RibRBacillus subtilis--679916

CAS REGISTRY NUMBERCOMMENTARY
9032-82-0-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thalianaecotype Columbia680633--Manually annotated by BRENDA team
Bacillus subtilis-641247, 641254, 679888, 679916, 687408--Manually annotated by BRENDA team
Bacillus subtilismonofunctional enzyme641252--Manually annotated by BRENDA team
Bacillus subtilisRibC from wild-type strain 1012 and RibC820 from riboflavin-overproducing mitant strain RB52.ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity641253P54575UniprotManually annotated by BRENDA team
Bos taurus-641251--Manually annotated by BRENDA team
Corynebacterium ammoniagenes-392186, 641248--Manually annotated by BRENDA team
Homo sapiens-641257, 657963Q969G6UniprotManually annotated by BRENDA team
Homo sapiens-705886--Manually annotated by BRENDA team
Megasphaera elsdenii-641242, 641243--Manually annotated by BRENDA team
Mus musculus-705886--Manually annotated by BRENDA team
Neurospora crassacell wall lacking mutant641249--Manually annotated by BRENDA team
Nicotiana tabacumcv. Bright Yellow 2703642--Manually annotated by BRENDA team
Rattus norvegicus-641235, 641237, 641238, 641239, 641240, 641241, 641244, 641250, 641255--Manually annotated by BRENDA team
Saccharomyces cerevisiae-641236--Manually annotated by BRENDA team
Schizosaccharomyces pombe-641256O74866UniprotManually annotated by BRENDA team
Streptomyces davawensis-687408A3FM23SwissProtManually annotated by BRENDA team
Vigna radiata var. radiata-641245--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionHomo sapiens, Mus musculus-riboflavin kinase is a TNF-receptor-1 binding protein that couples TNF-receptor-1 to NADPH oxidase705886

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dATP + riboflavin2'-dADP + riboflavin 5'-phosphate
show the reaction diagram		Corynebacterium ammoniagenes--641248--?
2'-dATP + riboflavin2'-dADP + riboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-50% of the activity with ATP641235--?
adenosine-5'-O-(3-thiotriphosphate) + riboflavin?
show the reaction diagram		Rattus norvegicus-48% of the activity with ATP641235--?
ADP + riboflavinAMP + FMN
show the reaction diagram		Megasphaera elsdenii-22% of the activity with ATP641242, 641243--?
ATP + 10-(D-allo)flavinADP + 10-(D-allo)flavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-30% of the activity with riboflavin641241--?
ATP + 10-(L-arabo)flavinADP + 10-(L-arabo)flavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-25% of the activity with riboflavin641241--?
ATP + 2'-deoxyriboflavinADP + 2'-deoxyriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-31% of the activity with riboflavin641240--?
ATP + 2-thioriboflavinADP + 2-thioriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-60% of the activity with riboflavin641241--?
ATP + 2-thioriboflavinADP + 2-thioriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-30% of the activity with riboflavin641244---
ATP + 3-deazariboflavinADP + 3-deazariboflavin 5'-phosphate
show the reaction diagram		Corynebacterium ammoniagenes--392186--?
ATP + 3-methylriboflavinADP + 3-methylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-5% of the activity with riboflavin641244--?
ATP + 5-deazariboflavinADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram		Bacillus subtilis--641247--?
ATP + 5-deazariboflavinADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram		Megasphaera elsdenii--641243--?
ATP + 5-deazariboflavinADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram		Corynebacterium ammoniagenes--392186--?
ATP + 5-deazariboflavinADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram		Megasphaera elsdenii-15% of the activity with riboflavin641242--?
ATP + 5-deazariboflavinADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-as active as riboflavin641244---
ATP + 5-methyl-5-deazariboflavinADP + 5-methyl-5-deazariboflavin 5'-phosphate
show the reaction diagram		Corynebacterium ammoniagenes--392186--?
ATP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazineADP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazine phosphate
show the reaction diagram		Saccharomyces cerevisiae-35% of the activity with riboflavin641236--?
ATP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazineADP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazine phosphate
show the reaction diagram		Rattus norvegicus-52% of the activity with riboflavin641238---
ATP + 6,7-dimethyl-9-(1'-D-ribityl)-2-iminoisoalloxazineADP + 6,7-dimethyl-9-(1'-D-ribityl)-2-iminoisoalloxazine 5'-phosphate
show the reaction diagram		Rattus norvegicus-18% of the activity with riboflavin641238--?
ATP + 6-methylriboflavinADP + 6-methylriboflavin 5'-phosphate
show the reaction diagram		Corynebacterium ammoniagenes--392186--?
ATP + 7-chlororiboflavinADP + 7-chlororiboflavin
show the reaction diagram		Corynebacterium ammoniagenes--392186--?
ATP + 8-bromo-8-demethylriboflavinADP + 8-bromo-8-demethylriboflavin 5-'phosphate
show the reaction diagram		Rattus norvegicus-384% of the activity with riboflavin641240--?
ATP + 8-chloro-8-demethylriboflavinADP + 8-chloro-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-122.2% of the activity with riboflavin641240--?
ATP + 8-demethylriboflavinADP + 8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-35% of the activity with riboflavin641241--?
ATP + 8-demethylriboflavinADP + 8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-110% of the activity with riboflavin641240--?
ATP + 8-dimethylamino-8-demethylriboflavinADP + 8-dimethylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-110% of the activity with riboflavin641240--?
ATP + 8-dimethylamino-8-demethylriboflavinADP + 8-dimethylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-70% of the activity with riboflavin641241--?
ATP + 8-ethoxy-8-demethylriboflavinADP + 8-ethoxy-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-210% of the activity with riboflavin641240--?
ATP + 8-fluoro-8-demethylriboflavinADP + 8-fluoro-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-132.2% of the activity with riboflavin641240--?
ATP + 8-iodo-8-demethylriboflavinATP + 8-iodo-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-334.7% of the activity with riboflavin641240--?
ATP + 8-methoxy-8-demethylriboflavinADP + 8-methoxy-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-114.5% of the activity with riboflavin641240--?
ATP + 8-methylamino-8-demethylriboflavinATP + 8-methylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-237.3% of the activity with riboflavin641240--?
ATP + 9-azariboflavinADP + 9-azariboflavin 5'-phosphate
show the reaction diagram		Corynebacterium ammoniagenes--392186--?
ATP + alloflavinADP + alloflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus--641237--?
ATP + arabitylflavinADP + arabitylflavin phosphate
show the reaction diagram		Rattus norvegicus-14% of the activity with riboflavin641238--?
ATP + arabitylflavinADP + arabitylflavin phosphate
show the reaction diagram		Saccharomyces cerevisiae-slightly more active than riboflavin641236--?
ATP + D-erythroflavinADP + D-erythroflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus--641235---
ATP + D-erythroflavinADP + D-erythroflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus--641237--?
ATP + D-erythroflavinADP + D-erythroflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-10-(D-erythro)flavin, 33% of the activity with riboflavin641241--?
ATP + riboflavinADP + FMN
show the reaction diagram		Vigna radiata var. radiata--641245--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis--641247, 641252--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilisP54575-641253--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis--679916, 687408--?
ATP + riboflavinADP + FMN
show the reaction diagram		Homo sapiensQ969G6-641257--?
ATP + riboflavinADP + FMN
show the reaction diagram		Homo sapiens--657963--ir
ATP + riboflavinADP + FMN
show the reaction diagram		Rattus norvegicus--641235, 641237, 641238, 641239, 641240, 641241, 641244, 641250, 641255--?
ATP + riboflavinADP + FMN
show the reaction diagram		Saccharomyces cerevisiae--641236--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bos taurus--641251--?
ATP + riboflavinADP + FMN
show the reaction diagram		Neurospora crassa--641249--?
ATP + riboflavinADP + FMN
show the reaction diagram		Arabidopsis thaliana--680633--?
ATP + riboflavinADP + FMN
show the reaction diagram		Schizosaccharomyces pombeO74866-641256--?
ATP + riboflavinADP + FMN
show the reaction diagram		Megasphaera elsdenii--641242, 641243--?
ATP + riboflavinADP + FMN
show the reaction diagram		Corynebacterium ammoniagenes--392186, 641248--?
ATP + riboflavinADP + FMN
show the reaction diagram		Streptomyces davawensisA3FM23-687408--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis-specific for the reduced form of riboflavin641254--?
ATP + riboflavinADP + FMN
show the reaction diagram		Homo sapiensQ969G6essential enzyme catalyzing the phosphorylation of riboflavin to form FMN, an obligatory step in vitamin B2 utilization and flavin cofactor synthesis641257--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis-key enzyme in flavin biosynthesis641252--?
ATP + riboflavinADP + FMN
show the reaction diagram		Neurospora crassa-key enzyme in flavin biosynthesis641249--?
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilisP54575ribC is essential for growth of Bacillus subtilis. RibC is not directly involved in the riboflavin regulatory system641253--?
ATP + riboflavinADP + FMN
show the reaction diagram		Homo sapiens-substrate and product binding structure, overview657963--ir
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis-the flavokinase activity appears to be localized to the N-terminal domain of the protein. RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. In RibR itself, interaction was localized to the carboxy-terminate part of the protein679916--?
ATP + roseoflavinADP + roseoflavin 5'-phosphate
show the reaction diagram		Bacillus subtilis--687408--?
ATP + roseoflavinADP + roseoflavin 5'-phosphate
show the reaction diagram		Streptomyces davawensisA3FM23-687408--?
ATP + roseoflavinADP + roseoflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-187% of the activity with 8-demethylriboflavin641240--?
ATP + roseoflavinADP + roseoflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-enzyme from intestinal mucosa and liver641235--?
ATP + roseoflavinADP + roseoflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-81% of the activity with riboflavin641240--?
ATP + roseoflavinADP + roseoflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-90% of the activity with riboflavin641244--?
CTP + riboflavinCTP + riboflavin 5'-phosphate
show the reaction diagram		Bacillus subtilis-50% of the activity with ATP641252--?
CTP + riboflavinCTP + riboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-39% of the activity with ATP641235--?
dATP + riboflavindADP + FMN
show the reaction diagram		Bacillus subtilis--641252--?
dATP + riboflavindADP + FMN
show the reaction diagram		Rattus norvegicus--641241--?
GTP + riboflavinGTP + riboflavin 5'-phosphate
show the reaction diagram		Megasphaera elsdenii-no activity641242, 641243---
riboflavin + ATPFMN + ADP
show the reaction diagram		Nicotiana tabacum--703642--?
UTP + riboflavinUDP + FMN
show the reaction diagram		Rattus norvegicus-UTP is a poor substrate641235--?
UTP + riboflavinUDP + FMN
show the reaction diagram		Bacillus subtilis-31% of the activity with ATP641252--?
GTP + riboflavinGTP + riboflavin 5'-phosphate
show the reaction diagram		Rattus norvegicus-35% of the activity with ATP641235--?
additional information?-Rattus norvegicus-analogs of riboflavin modified at position 8 seem to be good substrates, analogs modified at position 3 are not phosphorylated641235---
additional information?-Bacillus subtilisP54575ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity641253---
additional information?-Saccharomyces cerevisiae-no phosphorylation of isoriboflavin, galactoflavin, dulcitylflavin, sorbitylflavin641236---
additional information?-Bacillus subtilis-the riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product679888---
additional information?-Streptomyces davawensisA3FM23the bifunctional flavokinase/flavin adenine dinucleotide synthetase produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin687408---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + riboflavinADP + FMN
show the reaction diagram		Homo sapiens--657963--
ATP + riboflavinADP + FMN
show the reaction diagram		Homo sapiensQ969G6essential enzyme catalyzing the phosphorylation of riboflavin to form FMN, an obligatory step in vitamin B2 utilization and flavin cofactor synthesis641257--
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis-key enzyme in flavin biosynthesis641252--
ATP + riboflavinADP + FMN
show the reaction diagram		Neurospora crassa-key enzyme in flavin biosynthesis641249--
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilisP54575ribC is essential for growth of Bacillus subtilis. RibC is not directly involved in the riboflavin regulatory system641253--
ATP + riboflavinADP + FMN
show the reaction diagram		Bacillus subtilis-the flavokinase activity appears to be localized to the N-terminal domain of the protein. RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. In RibR itself, interaction was localized to the carboxy-terminate part of the protein679916--
additional information?-Bacillus subtilis-the riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product679888--
additional information?-Streptomyces davawensisA3FM23the bifunctional flavokinase/flavin adenine dinucleotide synthetase produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin687408--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Cd2+Corynebacterium ammoniagenes-38% of the activation with Zn2+641248
Co2+Bacillus subtilis-0.1 mM, activation is about 65% of that with 0.2 mM Mg2+641247
Co2+Corynebacterium ammoniagenes-34% of the activation with Zn2+641248
Co2+Neurospora crassa-divalent metal ions are essential activators, in the order of decreasing efficiency: Mg2+, Co2+, Zn2+, Cu2+, Cd2+, Fe2+641249
Mg2+Rattus norvegicus-enhances activity641235
Mg2+Rattus norvegicus-activates641241
Mg2+Bacillus subtilis-0.2 mM, Mg2+ or Zn2+ required641247
Mg2+Corynebacterium ammoniagenes-38% of the activation with Zn2+641248
Mg2+Neurospora crassa-most effective essential activator641249
Mg2+Bacillus subtilis-required for maximal activity641252
Mg2+Homo sapiens--657963
Mn2+Bacillus subtilis-activation is about 45% of that with 0.2 mM Mg2+641247
Mn2+Corynebacterium ammoniagenes-31% of the activation with Zn2+641248
Zn2+Rattus norvegicus-enhances activity, more effective than Mg2+641235
Zn2+Rattus norvegicus-activation is 1.8times of that with Mg2+641241
Zn2+Bacillus subtilis-activation is about 90% of that with 0.2 mM Mg2+641247
Zn2+Corynebacterium ammoniagenes-best divalent metal activator641248
Zn2+Bacillus subtilis-less effective in activation than Mg2+641252

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1'-DL-glyceryl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
1-DeazariboflavinRattus norvegicus--641241 2D-image
10-(2'-Hydroxyethyl)-isoalloxazineBacillus subtilis-0.01 mM, 34% inhibition641247 2D-image
10-(4'-Carboxybutyl)-isoalloxazineBacillus subtilis-0.001 mM, 16% inhibition641247 2D-image
10-(5'-Hydroxypentyl)-isoalloxazineBacillus subtilis-0.01 mM, 38% inhibition641247 2D-image
10-(5'-Hydroxypentyl)flavinRattus norvegicus--641241 2D-image
10-(Hydroxyethyl)flavinRattus norvegicus--641241 2D-image
2'-ThioriboflavinBacillus subtilis-0.01 mM, 59% inhibition641247 2D-image
3'-hydroxypropyl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
3-DeazariboflavinRattus norvegicus--641241 2D-image
3-methylriboflavinBacillus subtilis-0.01 mM, 5% inhibition641247 2D-image
4'-hydroxybutyl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
5'-hydroxypentyl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
5-DeazariboflavinRattus norvegicus--641241 2D-image
7,8-dimethyl-10-(2'-hydroxyethyl)-isoalloxazineBacillus subtilis-0.5 mM, 10% inhibition641252 2D-image
7,8-dimethyl-10-(O-methylacetoxime)-isoaloxazineBacillus subtilis-0.5 mM, 34% inhibition641252 2D-image
7alpha-MethylriboflavinBacillus subtilis-0.01 mM, 95% inhibition641247 2D-image
8-AminoriboflavinRattus norvegicus--641241 2D-image
8-DiethylaminoriboflavinRattus norvegicus--641241 2D-image
8-EthoxyriboflavinRattus norvegicus--641241 2D-image
8-EthylaminoriboflavinRattus norvegicus--641241 2D-image
8-hydroxyriboflavinRattus norvegicus--641241 2D-image
8-MethoxyriboflavinRattus norvegicus--641241 2D-image
8-MethylaminoriboflavinRattus norvegicus--641241 2D-image
8-MethylethylaminoriboflavinRattus norvegicus--641241 2D-image
9-(6'-hydroxyhexyl)-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
Ba2+Rattus norvegicus--641241 2D-image
Ca2+Bacillus subtilis--641252 2D-image
Cd2+Rattus norvegicus-maximum inhibition at 1 mM641250 2D-image
Cd2+Rattus norvegicus-78% inhibition at 1 mM, effect is completely reversed by increasing concentrations of Zn2+, protection by glutathione and dithiothreitol641255 2D-image
Co2+Bacillus subtilis--641252 2D-image
Cu2+Rattus norvegicus-maximum inhibition at 1 mM641250 2D-image
Cu2+Rattus norvegicus--641255 2D-image
DTNBRattus norvegicus--641250 2D-image
Fe2+Rattus norvegicus--641241 2D-image
FMNRattus norvegicus-product inhibition641239 2D-image
Hg2+Rattus norvegicus-0.1 mM, complete inhibition641250 2D-image
Hg2+Rattus norvegicus--641255 2D-image
lumichromeRattus norvegicus--641241 2D-image
LumiflavinRattus norvegicus--641241 2D-image
LumiflavinBacillus subtilis-0.01 mM, 38% inhibition641247 2D-image
LumiflavinBacillus subtilis-0.5 mM, 4% inhibition641252 2D-image
NEMRattus norvegicus--641250 2D-image
PCMBRattus norvegicus-1 mM, 70% inhibition641250 2D-image
PCMBRattus norvegicus--641255 2D-image
Riboflavin 5'-phosphateRattus norvegicus--641241 2D-image
roseoflavinBacillus subtilis-0.4 mM, 8% inhibition641252 2D-image
Sr2+Rattus norvegicus--641241 2D-image
ZnADP-Rattus norvegicus-product inhibition641239 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
CarbonateNeurospora crassa-50 mM, activates641249 2D-image
NO3-Neurospora crassa-50 mM, activates641249 2D-image
phosphateNeurospora crassa-50 mM, activates641249 2D-image
SO42-Neurospora crassa-50 mM, activates641249 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.025-adenosine-5'-O-(3-thiotriphosphate)Rattus norvegicus--641235 2D-image
0.0002-ATPArabidopsis thaliana-bifunctional enzyme AtFMN/FHy680633 2D-image
0.0037-ATPRattus norvegicus--641235 2D-image
0.0065-ATPBacillus subtilis--641247 2D-image
0.008-ATPRattus norvegicus-enzyme from brain641235 2D-image
0.0083-ATPBos taurus-pH 7.0, 25°C641251 2D-image
0.112-ATPBacillus subtilis-pH 8, 37°C641252 2D-image
0.2-ATPRattus norvegicus-pH 8, 37°C641244 2D-image
4.55-ATPRattus norvegicus--641255 2D-image
0.0015-D-alloflavinRattus norvegicus--641235 2D-image
0.0011-D-erythroflavinRattus norvegicus--641235 2D-image
0.0012-D-riboflavinRattus norvegicus--641235 2D-image
2.1e-05-MgATP2-Neurospora crassa-pH 8.5, 30°C641249 2D-image
0.005-MgATP2-Corynebacterium ammoniagenes--641248 2D-image
1.03e-05-riboflavinArabidopsis thaliana-bifunctional enzyme AtFMN/FHy680633 2D-image
0.00012-riboflavinNeurospora crassa-pH 8.5, 30°C641249 2D-image
0.00032-riboflavinNicotiana tabacum-allosteric kinetics703642 2D-image
0.0047-riboflavinMegasphaera elsdenii--641242 2D-image
0.0047-riboflavinMegasphaera elsdenii-pH 7.2, 37°C641243 2D-image
0.009-riboflavinRattus norvegicus--641235 2D-image
0.01-riboflavinRattus norvegicus-pH 8.0, 37°C641241 2D-image
0.01-riboflavinMegasphaera elsdenii--641242 2D-image
0.01-riboflavinMegasphaera elsdenii-pH 7.2, 37°C641243 2D-image
0.01-riboflavinRattus norvegicus-pH 8.0, 37°C641244 2D-image
0.011-riboflavinRattus norvegicus--641239 2D-image
0.0153-riboflavinBos taurus-pH 7.0, 25°C641251 2D-image
0.04-riboflavinStreptomyces davawensisA3FM2337°C687408 2D-image
0.055-riboflavinBacillus subtilis-37°C687408 2D-image
0.18-riboflavinBacillus subtilis-pH 8, 37°C641252 2D-image
0.03-roseoflavinBacillus subtilis-37°C687408 2D-image
0.03-roseoflavinStreptomyces davawensisA3FM2337°C687408 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.1-MgATP2-Neurospora crassa-pH 8.5, 30°C641249 2D-image
0.1-riboflavinNeurospora crassa-pH 8.5, 30°C641249 2D-image
0.3-riboflavinStreptomyces davawensisA3FM2337°C687408 2D-image
0.7-riboflavinBacillus subtilis-37°C687408 2D-image
0.4-roseoflavinBacillus subtilis-37°C687408 2D-image
0.5-roseoflavinStreptomyces davawensisA3FM2337°C687408 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0065-1'-DL-glyceryl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
0.021-1-DeazariboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.008-10-(5'-Hydroxypentyl)flavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.007-10-(Hydroxyethyl)flavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.0071-3'-hydroxypropyl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
0.41-3-DeazariboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.0076-4'-hydroxybutyl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
0.0078-5'-hydroxypentyl-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
0.275-5-DeazariboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.25-8-AminoriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.02-8-DiethylaminoriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.016-8-EthoxyriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.175-8-EthylaminoriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.5-8-hydroxyriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.015-8-MethoxyriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.47-8-MethylaminoriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.03-8-MethylethylaminoriboflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.0079-9-(6'-hydroxyhexyl)-6,7-dimethylisoalloxazineRattus norvegicus-competitive641237 2D-image
0.006-FMNRattus norvegicus-pH 8.0, 37°C, against riboflavin641239 2D-image
0.01-lumichromeRattus norvegicus-pH 8, 37°C641241 2D-image
0.007-LumiflavinRattus norvegicus-pH 8, 37°C641241 2D-image
0.018-Riboflavin 5'-phosphateRattus norvegicus-pH 8, 37°C641241 2D-image
0.023-ZnADP-Rattus norvegicus-pH 8.0, 37°C, against ZnATP2-641239 2D-image
0.12-ZnADP-Rattus norvegicus-pH 8.0, 37°C, against riboflavin641239 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.00023-Rattus norvegicus--641250
0.0083-Megasphaera elsdenii--641242
0.0083-Megasphaera elsdenii-continuous fluorometric assay641243
0.0129-Bacillus subtilis--641247
0.165-Rattus norvegicus--641241
0.322-Vigna radiata var. radiata--641245
0.716-Rattus norvegicus-enzyme from brain641235
0.79-Rattus norvegicus--641240
2.95-Neurospora crassa--641249
additional information-Bos taurus-bioluminescent assay641251

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7-Megasphaera elsdenii--641243
7-Bos taurus--641251
8.59Vigna radiata var. radiata-Tris-HCl buffer641245
8.59Neurospora crassa--641249
8.5-Bacillus subtilis--641252
9-Rattus norvegicus-enzyme from brain641235
9-Rattus norvegicus-enzyme from intestinal mucosa641240

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
58.5Megasphaera elsdenii-enzyme is active between pH 5 and 8.5641243
59Bos taurus-pH 5.0: about 30% of maximal activity, pH 9.0: about 65% of maximal activity641251

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
35-Bos taurus--641251
3757Neurospora crassa--641249
5055Vigna radiata var. radiata--641245
52-Bacillus subtilis--641252
60-Rattus norvegicus--641240

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1545Bos taurus-15°C: about 60% of maximal activity, 45°C: about 75% of maximal activity641251
2045Megasphaera elsdenii-the relative activities at pH 7.2 and 20°C, 25°C, 37°C and 45°C are 0.22, 0.46, 1, and 1.35, respectively641242, 641243

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainRattus norvegicus--641235Manually annotated by BRENDA team
HeLa cellHomo sapiens--705886Manually annotated by BRENDA team
intestinal mucosaRattus norvegicus--641235, 641240Manually annotated by BRENDA team
liverRattus norvegicus--641235, 641237, 641238, 641239, 641241, 641244, 641250, 641255Manually annotated by BRENDA team
liverBos taurus--641251Manually annotated by BRENDA team
MEF cellMus musculus--705886Manually annotated by BRENDA team
seedVigna radiata var. radiata--641245Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
mitochondrionNicotiana tabacum--5739703642Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3zug, downloadSCOP (3zug)CATH (3zug)Corynebacterium ammoniagenes
1nb0, downloadSCOP (1nb0)CATH (1nb0)Homo sapiens
1nb9, downloadSCOP (1nb9)CATH (1nb9)Homo sapiens
1p4m, downloadSCOP (1p4m)CATH (1p4m)Homo sapiens
1q9s, downloadSCOP (1q9s)CATH (1q9s)Homo sapiens
1n05, downloadSCOP (1n05)CATH (1n05)Schizosaccharomyces pombe (strain 972 / ATCC 24843)
1n06, downloadSCOP (1n06)CATH (1n06)Schizosaccharomyces pombe (strain 972 / ATCC 24843)
1n07, downloadSCOP (1n07)CATH (1n07)Schizosaccharomyces pombe (strain 972 / ATCC 24843)
1n08, downloadSCOP (1n08)CATH (1n08)Schizosaccharomyces pombe (strain 972 / ATCC 24843)
3bnw, downloadSCOP (3bnw)CATH (3bnw)Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
13500-Rattus norvegicus-gel filtration641240
27000-Rattus norvegicus-gel filtration641241
27250-Bacillus subtilis-gel filtration641252
34200-Bacillus subtilisP54575gel filtration641253
35000-Vigna radiata var. radiata-gel filtration641245
35500-Neurospora crassa-gel filtration641249
40000-Corynebacterium ammoniagenes-gel filtration641248

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
monomerRattus norvegicus-1 * 13500, SDS-PAGE641240
monomerRattus norvegicus-1 * 28000, SDS-PAGE641241
monomerVigna radiata var. radiata-1 * 30000, SDS-PAGE641245
monomerCorynebacterium ammoniagenes-1 * 40000, SDS-PAGE641248
monomerNeurospora crassa-1 * 35500, SDS-PAGE641249
monomerBacillus subtilisP545751 * 36000, SDS-PAGE641253

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Homo sapiens-641257
purified recombinant enzyme with bound products FMN and MgADP, hanging drop vapour diffusion method, 34 mg/ml protein in 50 mM Tris, pH 7.4, 0.3 M NaCl, 1 mM DTT, 20°C, mixing with equal volume of reservoir solution containing 0.1 M sodium acetate, pH 4.7, 30% PEG monomethyl ether 5000, and 0.2 M ammonium sulfate, followed by microseeding in reservoir solution containing 0.1 M sodium acetate, pH 4.4, 22.5% PEG monomethyl ether 5000, and 0.2 M ammonium sulfate, cryoprotection in 30% glycerol in reservoir solution, storage in liquid propane, X-ray diffraction structure determination and analysis at 2.4 A resolutionHomo sapiens-657963
-Schizosaccharomyces pombeO74866641256

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
25-Rattus norvegicus-enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks641244

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
loss of activity during repeated freezing and thawingMegasphaera elsdenii-641243
50% of the activity is lost on freezing, but the stability of the enzyme is not greatly affected by the period of freezingRattus norvegicus-641240
enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks at 25°CRattus norvegicus-641244
enzyme is inactivated by freezing and thawing unless both riboflavin and 20% glycerol are addedRattus norvegicus-641241

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
3°C, MOPS buffer, activity decreases to approximately 35, 30 and 13% of the initial level after 24, 48, and 96 h, respectivelyRattus norvegicus-641240
4°C, 50% loss of activity after 2 d when the enzyme is stored in buffer alone, complete protection by 0.01 mM riboflavinRattus norvegicus-641241
purified enzyme is unstable in dilute solution and can not be stored at -20°CRattus norvegicus-641235

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacillus subtilis-641247
recombinant enzymeBacillus subtilisP54575641253
presence of ATP:riboflavin 5'-phosphotransferase and ATP:FMN adenylyltransferase on a single polypeptideCorynebacterium ammoniagenes-641248
recombinant, His-tagged enzyme by nickel affinity chromatography, removal of His-tag by TEV-protease treatmentHomo sapiens-657963
partial, affinity chromatographyMegasphaera elsdenii-641242
-Neurospora crassa-641249
-Rattus norvegicus-641241, 641255
enzyme from brainRattus norvegicus-641235
partialRattus norvegicus-641250
recombinant enzymeStreptomyces davawensisA3FM23687408
affinity chromatographyVigna radiata var. radiata-641245

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
the functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of AtFMN/FHyArabidopsis thaliana-680633
-Bacillus subtilis-679888, 679916
amplification, cloning and expression of ribR gene in Escherichia coli; expression of ribC gene in Escherichia coliBacillus subtilis-641254
expression of ribC gene in Escherichia coliBacillus subtilisP54575641253
expressed in Escherichis coli BL-21—pLysS (DE3), C-terminal glutathione S-transferase fusionproteinHomo sapiens-705886
expressed in Escherichia coliMus musculus-705886
overproduced in Escherichia coliStreptomyces davawensisA3FM23687408

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
E86QHomo sapiens-destroying the kinase domain, purified as C-terminal glutathione S-transferase fusionprotein705886
N36DHomo sapiens-purified as C-terminal glutathione S-transferase fusionprotein705886

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisRattus norvegicus-immobilized enzyme is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile method for preparing exclusively other synthetic methods, the 5'-phosphates641244

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
HypertensionImportance of Riboflavin Kinase in the Pathogenesis of Stroke. PubMed
InfectionFlavin metabolism during respiratory infection in mice. PubMed
NeoplasmsDeath receptors 4 and 5 activate Nox1 NADPH oxidase through riboflavin kinase to induce reactive oxygen species-mediated apoptotic cell death. PubMed
Prostatic NeoplasmsInvolvement of riboflavin kinase expression in cellular sensitivity against cisplatin. PubMed
Riboflavin DeficiencyEffect of riboflavin status on hepatic activities of flavin-metabolizing enzymes in rats. PubMed
StrokeImportance of Riboflavin Kinase in the Pathogenesis of Stroke. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
392186Walsh, C.; Fisher, J.; Spencer, R.; Graham, D.W.; Ashton, W.T.; Brown, J.E.; Brown, R.D.; Rogers, E.F.Chemical and enzymatic properties of riboflavin analoguesBiochemistry171942-19511978Corynebacterium ammoniagenes PubMed
641235Nakano, H.; McCormick, D.B.Rat brain flavokinase: purification, properties and comparison to the enzyme from liver and small intestineFlavins and Flavoproteins (Proc. Int. Symp., 10th, Meeting Date 1990, Curti, B., Ronchi S., Zanetti, G., eds.) de Gruyter, BerlinNew York89-921991Rattus norvegicus-
641236Kearney, E.B.The interaction of yeast flavokinase with riboflavin analoguesJ. Biol. Chem.194747-7541952Saccharomyces cerevisiae PubMed
641237Chassy, B.M.; Arsenis, C.; McCormick, D.B.The effect of the length of the side chain of flavins on reactivity with flavokinaseJ. Biol. Chem.2401338-13401965Rattus norvegicus PubMed
641238McCormick, D.B.; Butler, R.C.Substrate specificity of liver flavokinaseBiochim. Biophys. Acta65326-3321962Rattus norvegicus-
641239Yamada, Y.; Merrill, A.; McCormick, D.N.Probable reaction mechanisms of flavokinase and FAD synthetase from rat liverArch. Biochem. Biophys.278125-1301990Rattus norvegicus PubMed
641240Kasai, S.; Nakano, H.; Maeda, K.; Matsui, K.Purification, properties, and function of flavokinase from rat intestinal mucosaJ. Biochem.107298-3031990Rattus norvegicus PubMed
641241Merrill, A.H.; McCormick, D.B.Affinity chromatographic purification and properties of flavokinase (ATP:riboflavin 5-phosphotransferase) from rat liverJ. Biol. Chem.2551335-13381980Rattus norvegicus PubMed
641242Mayhew, S.G.; Wassink, J.H.Continuous fluorescence assay, partial purification and properties of flavokinase from Megasphaera elsdeniiMethods Enzymol.66323-3271980Megasphaera elsdenii PubMed
641243Mayhew, S.G.; Wassink, J.H.A continuous fluorometric assay for flavokinase. Properties of flavokinase from Peptostreptococcus elsdeniiBiochim. Biophys. Acta482341-3471977Megasphaera elsdenii PubMed
641244Merrill, A.H.; McCormick, D.B.Preparation and properties of immobilized flavokinaseBiotechnol. Bioeng.211629-16381979Rattus norvegicus PubMed
641245Sobhanaditya, J.; Rao, N.A.Plant flavokinase. Affinity-chromatographic procedure for the purification of the enzyme from mung-bean (Phaseolus aureus) seeds and conformational changes on its interaction with orthophosphateBiochem. J.197227-2321981Vigna radiata var. radiata PubMed
641247Kearny, E.B.; Goldenberg, J.; Lipsick, J.; Perl, M.Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavinsJ. Biol. Chem.2549551-95571979Bacillus subtilis PubMed
641248Manstein, D.J.; Pai, E.F.Purification and characterization of FAD synthetase from Brevibacterium ammoniagenesJ. Biol. Chem.26116169-161731986Corynebacterium ammoniagenes PubMed
641249Rajeswari, S.R.; Jonnalagadda, V.S.; Jonnalagadda, S.Purification and characterization of flavokinase from Neurospora crassaIndian J. Biochem. Biophys.36137-1421999Neurospora crassa PubMed
641250Bandyopadhyay, D.; Chatterjee, A.K.; Datta, A.G.Effect of cadmium, mercury and copper on partially purified hepatic flavokinase of ratMol. Cell. Biochem.16773-801997Rattus norvegicus PubMed
641251Cho, K.W.Bioluminescent assay of bovine liver riboflavin kinase using a bacterial luciferase coupled reactionJ. Microbiol.3874-792000Bos taurus-
641252Solovieva, I.M.; Tarasov, K.V.; Perumov, D.A.Main physicochemical features of monofunctional flavokinase from Bacillus subtilisBiochemistry68177-1812003Bacillus subtilis PubMed
641253Mack, M.; van Loon, A.P.; Hohmann, H.P.Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribCJ. Bacteriol.180950-9551998Bacillus subtilis PubMed
641254Solovieva, I.M.; Kreneva, R.A.; Leak, D.J.; Perumov, D.A.The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operonMicrobiology14567-731999Bacillus subtilis PubMed
641255Bandyopadhyay, D.; Chatterjee, A.K.; Datta, A.G.Effect of cadmium on purified hepatic flavokinase: involvement of reactive -SH group(s) in the inactivation of flavokinase by cadmiumLife Sci.601891-19031997Rattus norvegicus PubMed
641256Bauer, S.; Kemter, K.; Bacher, A.; Huber, R.; Fischer, M.; Steinbacher, S.Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding foldJ. Mol. Biol.3261463-14732003Schizosaccharomyces pombe PubMed
641257Karthikeyan, S.; Zhou, Q.; Mseeh, F.; Grishin, N.V.; Osterman, A.L.; Zhang, H.Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site archStructure11265-2732003Homo sapiens PubMed
657963Karthikeyan, S.; Zhou, Q.; Osterman, A.L.; Zhang, H.Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanismBiochemistry4212532-125382003Homo sapiens PubMed
679888Solovieva, I.M.; Kreneva, R.A.; Errais Lopes, L.; Perumov, D.A.The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene productFEMS Microbiol. Lett.24351-582005Bacillus subtilis PubMed
679916Higashitsuji, Y.; Angerer, A.; Berghaus, S.; Hobl, B.; Mack, M.RibR, a possible regulator of the Bacillus subtilis riboflavin biosynthetic operon, in vivo interacts with the 5-untranslated leader of rib mRNAFEMS Microbiol. Lett.27448-542007Bacillus subtilis PubMed
680633Sandoval, F.J.; Roje, S.An FMN hydrolase is fused to a riboflavin kinase homolog in plantsJ. Biol. Chem.28038337-383452005Arabidopsis thaliana PubMed
687408Grill, S.; Busenbender, S.; Pfeiffer, M.; Koehler, U.; Mack, M.The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavinJ. Bacteriol.1901546-15532008Bacillus subtilis, Streptomyces davawensis PubMed
703642Giancaspero, T.A.; Locato, V.; de Pinto, M.C.; De Gara, L.; Barile, M.The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox statusFEBS J.276219-2312009Nicotiana tabacum PubMed
705886Yazdanpanah, B.; Wiegmann, K.; Tchikov, V.; Krut, O.; Pongratz, C.; Schramm, M.; Kleinridders, A.; Wunderlich, T.; Kashkar, H.; Utermoehlen, O.; Bruening, J.C.; Schuetze, S.; Kroenke, M.Riboflavin kinase couples TNF receptor 1 to NADPH oxidaseNature4601159-11632009Homo sapiens, Mus musculus PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.26)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)