Literature summary for 2.7.1.26 extracted from

Anoz-Carbonell, E.; Rivero, M.; Polo, V.; Velazquez-Campoy, A.; Medina, M.
Human riboflavin kinase species-specific traits in the biosynthesis of the FMN cofactor (2020), FASEB J., 34, 10871-10886 .

Search for more literature for 2.7.1.26

Application

Application	Comment	Organism
drug development	HsRFK parameters differ from those of the so far evaluated bacterial counterparts, suggesting species-specific mechanisms in RFK catalysis. Thus, HsRFK is a potential therapeutic target because of its key functions, while bacterial RFK modules are potential antimicrobial targets	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
gene RFK, recombinant expression of His-tagged enzyme from codon-optimzed gene in Escherichia coli strain BL21(DE3)	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of the crystallographic structure of HsRFK in complex with FMN and ADP in either the open (PDB ID 1P4M) or the closed conformation (PDB ID 1Q9S) of the flavin binding site overview	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
ADP	product inhibition, fitted to the Lineweaver-Burk equation for competitive inhibition	Homo sapiens
FMN	product inhibition, fitted to the Lineweaver-Burk equation for competitive inhibition	Homo sapiens
additional information	the inhibition mechanism of the products of the RFK reaction, FMN and ADP, kinetics, overview	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics and modeling, cooperativity model, pre-steady-state kinetics/pre-steady-state stopped-flow kinetics and dissociation constants, overview. Isothermal titration calorimetry, and Gibbs free energy flow for the interaction of HsRFK with substrates and products. Thermodynamics modulates the ligand binding landscape of HsRFK. Cooperativity coefficients, ANP and FLV ligands cooperate in their binding to HsRFK	Homo sapiens
0.0025	-	riboflavin	pH 7.0, 25°C, recombinant enzyme	Homo sapiens
0.03	-	ATP	pH 7.0, 25°C, recombinant enzyme	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + riboflavin	Homo sapiens	-	ADP + FMN	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q969G6	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme RFK from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by a protease, followed by ammonium sulfate fractionation, hydrophobic interaction chromatography, and dialysis. HsRFK is purified free of flavin and adenine ligands	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + riboflavin	-	Homo sapiens	ADP + FMN	-	?
additional information	substrate binding structure analysis using crystal structures of substrate-bound RFK. Binding of HsRFK substrates is the kinetically preferred process compared to product inhibition, kinetic modeling, overview	Homo sapiens	?	-	-

Subunits

Subunits	Comment	Organism
More	structure-function analysis, apo-HsRFK structural model	Homo sapiens

Synonyms

Synonyms	Comment	Organism
HsRFK	-	Homo sapiens
RFK	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.7	-	ATP	pH 7.0, 25°C, recombinant enzyme	Homo sapiens
1.7	-	riboflavin	pH 7.0, 25°C, recombinant enzyme	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Homo sapiens

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	inhibition kinetics, recombinant enzyme, overview	Homo sapiens
0.0025	-	FMN	pH 7.0, 25°C, recombinant enzyme	Homo sapiens
0.033	-	ADP	pH 7.0, 25°C, recombinant enzyme	Homo sapiens

General Information

General Information	Comment	Organism
evolution	different organisms, different regulatory strategies of RFKs, overview	Homo sapiens
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	Homo sapiens
additional information	molecular dynamics simulations, structure-function analysis	Homo sapiens
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	Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
56.67	-	ATP	pH 7.0, 25°C, recombinant enzyme	Homo sapiens
680	-	riboflavin	pH 7.0, 25°C, recombinant enzyme	Homo sapiens

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Release 2023.1 (January 2023)