2.7.1.26: riboflavin kinase
This is an abbreviated version!
For detailed information about riboflavin kinase, go to the full flat file.
Word Map on EC 2.7.1.26
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2.7.1.26
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mononucleotide
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ammoniagenes
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fadss
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isoalloxazine
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kyphoplasty
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flavocoenzyme
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flavinogenic
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ribityl
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davawensis
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roseoflavin
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famata
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ctp-dependent
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synthesis
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drug development
- 2.7.1.26
- mononucleotide
- ammoniagenes
-
fadss
- isoalloxazine
-
kyphoplasty
-
flavocoenzyme
-
flavinogenic
-
ribityl
- davawensis
- roseoflavin
- famata
-
ctp-dependent
- synthesis
- drug development
Reaction
Synonyms
AtFMN/FHy, ATP: riboflavin kinase, ATP:riboflavin kinase, bifunctional riboflavin kinase/FMN adenylyltransferase, CaFADS, FAD synthetase, FADS, FK, flavokinase, flavokinase/FAD synthetase, flavokinase/flavin adenine dinucleotide synthetase, FMN adenylyltransferase, FMNAT, HsRFK, kinase, riboflavin, More, RFK, RibC, ribF, riboflavin kinase, riboflavin kinase/FMN adenylyltransferase, riboflavine kinase, RibR
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General Information on EC 2.7.1.26 - riboflavin kinase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
enzyme RFK downregulation alters expression profiles of clock-controlled metabolic-genes and destroys flavins protection on stroke treatments, while its activity reduction links to protein-energy malnutrition and thyroid hormones decrease
metabolism
biosynthesis of FMN and FAD from riboflavin (RF) involves two reactions: RF is first phosphorylated to FMN in an ATP-Mg2+-dependent reaction carried out by an ATP:riboflavin kinase (RFK), and then an FMN:ATP adenylyltransferase (FMNAT) transfers the adenylyl group from a second ATP molecule to FMN to yield FAD. In eukaryotes, these reactions are preferentially performed by two independent monofunctional enzymes, but in most prokaryotes, the two reactions are sequentially catalyzed by a bifunctional enzyme known as prokaryotic type I FAD synthetase (FADS). These bifunctional proteins are organized in two nearly independent modules with each one catalyzing one of the two activities
physiological function
additional information
evolution
eukaryotic FMNAT is related to phosphoadenosine phosphosulfate (PAPS) reductase family proteins and contains a core domain with a modified Rossman-fold topology and a C-terminal extension
evolution
whereas the N-terminal module of FADS lacks structural homology to eukaryotic FMNATs, the kinase module is homologous to monofunctional RFKs
evolution
different organisms, different regulatory strategies of RFKs, overview
physiological function
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riboflavin kinase is a TNF-receptor-1 binding protein that couples TNF-receptor-1 to NADPH oxidase
physiological function
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riboflavin kinase is a TNF-receptor-1 binding protein that couples TNF-receptor-1 to NADPH oxidase
physiological function
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the enzyme plays a critical role in the KD548-Fc-mediated reactive oxygen species accumulation and downstream signaling. The enzyme is essential in recruiting Nox1 to death receptor4/5
physiological function
flavocoenzymes, including flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), are versatile redox cofactors involved in many fundamental cellular processes in all living organisms. FAD is synthesized from riboflavin obtained from the diet via two enzymatic steps catalyzed by riboflavin kinase (RFK, EC 2.7.1.26) and essential FMN adenylyltransferase (FMNAT,EC 2.7.7.2). Phosphorylation of riboflavin by RFK is crucial for specific absorption of the vitamin and is the physiologically rate-limiting step in the biosynthesis of flavocoenzymes, whereas product (FAD) feedback inhibition is observed for mammalian FMNAT, suggesting that biosynthesis of FAD is also regulated at the FMNAT reaction step
physiological function
the essential cofactors of flavoproteins and flavoenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), are synthesized from riboflavin in two sequential reactions: riboflavin phosphorylation is catalysed by an ATP-riboflavin kinase (RFK, EC 2.7.1.26) to produce FMN, which can be then converted to FAD by an FMN:ATP adenylyltranferase (FMNAT, EC 2.7.7.2). Bacteria contain a single bifunctional polypeptide called FAD synthetase (FADS)
physiological function
Enzymes known as bifunctional and bimodular prokaryotic type-I FAD synthetase (FADS) exhibit ATP:riboflavin kinase (RFK) and FMN:ATP adenylyltransferase (FMNAT) activities in their C-terminal and N-terminal modules, respectively, and produce flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). These act as cofactors of a plethora of flavoproteins in all organisms. Kinetics and thermodynamics of the protein-ligand interactions of riboflavin kinase activity of FAD synthetase from Corynebacterium ammoniagenes, overview. FMN synthesis is a key process that requires tight regulation. FMN production by CaFADS is highly regulated by substrate and product inhibition of its RFK activity to avoid overproduction even though the RF substrate might transiently increases in the media, where usually the amount of RF is considerably lower than that of FMN and particularly of FAD (either free or as part of flavoproteins)
physiological function
human riboflavin kinase is an essential enzyme that catalyzes the biosynthesis of the flavin mononucleotide (FMN) cofactor using riboflavin (RF, vitamin B2) and ATP as substrates. Human riboflavin kinase (HsRFK) catalyzes vitamin B2 (riboflavin) phosphorylation to flavin mononucleotide (FMN), obligatory step in flavin cofactor synthesis. HsRFK expression is related to protection from oxidative stress, amyloid-beta toxicity, and some malignant cancers progression. HsRFK is also predicted as involved in a protein-protein association network that at the system level affects to different cellular processes
additional information
molecular dynamics simulations of riboflavin kinase domain bound to FMN, ADP, and Mg2+, structure-function analysis, flavin-binding site structure in the RFK module of CaFADS, overview
additional information
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molecular dynamics simulations of riboflavin kinase domain bound to FMN, ADP, and Mg2+, structure-function analysis, flavin-binding site structure in the RFK module of CaFADS, overview
additional information
residue E268 is the catalytic base of the kinase reaction. The salt bridge between E268 at the RFK site and R66 at the FMNAT-module is important for the riboflavinkinase activity. Cross-talk between the RFK- and FMNAT-modules of neighboring protomers in the CaFADS enzyme, and participation of R66 in the modulation of the geometry of the RFK active site during catalysis
additional information
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residue E268 is the catalytic base of the kinase reaction. The salt bridge between E268 at the RFK site and R66 at the FMNAT-module is important for the riboflavinkinase activity. Cross-talk between the RFK- and FMNAT-modules of neighboring protomers in the CaFADS enzyme, and participation of R66 in the modulation of the geometry of the RFK active site during catalysis
additional information
adenine and flavin nucleotide ligands cooperate in their binding to the RFK module
additional information
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adenine and flavin nucleotide ligands cooperate in their binding to the RFK module
additional information
molecular dynamics simulations, structure-function analysis
additional information
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molecular dynamics simulations, structure-function analysis
