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
ECTree
Advanced search results
KM Value
KM Value on EC 2.7.1.26 - riboflavin kinase
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0.01
ATP
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.011
ATP
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.011
ATP
mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.012
ATP
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.012
ATP
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.012
ATP
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.012
ATP
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0137
ATP
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apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.014
ATP
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.014
ATP
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.014
ATP
wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0176
ATP
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apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.024
ATP
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.035
ATP
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.04
ATP
pH 7.0, 25°C, recombinant RFK activity of the RFK module, Lineweaver-Burk equation kinetics
0.0453
ATP
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apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.06
ATP
pH 7.0, 25°C, recombinant RFK activity of the RFK module, Michaelis-Menten kinetics
0.00089
riboflavin
mutant enzyme R66E, at pH 7.0 and 25°C
0.0017
riboflavin
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0021
riboflavin
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apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.0041
riboflavin
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apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.0045
riboflavin
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0056
riboflavin
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0069
riboflavin
pH 7.0, 25°C, recombinant RFK activity of the RFK module, Lineweaver-Burk equation kinetics
0.0077
riboflavin
mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0088
riboflavin
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.01
riboflavin
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.01
riboflavin
pH 7.0, 25°C, recombinant RFK activity of the RFK module, Michaelis-Menten kinetics
0.0117
riboflavin
pH 7.0, 25°C, recombinant wild-type enzyme
0.012
riboflavin
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.013
riboflavin
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apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.013
riboflavin
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.013
riboflavin
wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.016
riboflavin
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.023
riboflavin
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
0.025
riboflavin
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C
additional information
steady-state kinetic analysis of wild-type and mutant enzymes
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additional information
additional information
bi-substrate enzyme kinetics of the recombinant DELTA(1-182)CaFADS module
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additional information
additional information
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bi-substrate enzyme kinetics of the recombinant DELTA(1-182)CaFADS module
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additional information
additional information
Michaelis-Menten model and thermodynamic profiles of recombinant wild-type and mutant enzymes, overview
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additional information
additional information
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Michaelis-Menten model and thermodynamic profiles of recombinant wild-type and mutant enzymes, overview
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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
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additional information
additional information
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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
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additional information
additional information
Michaelis-Menten steady-state kinetic study. While Km ATP values increase with the ADP concentration, kcat values remain constant. The high affinity for the ADP product inhibitor considerably increases the estimated error for KmATP. Association and dissociation kinetics of flavin ligands to the RFK module are measured by flavin fluorescence changes, stopped-flow kinetics. Pre-steady-state kinetic analysis of the binding of flavins to the RFK module of CaFADS, thermodynamic diagram for the RFK-ligand interactions. Adenine and flavin nucleotide ligands cooperate in their binding to the RFK module. Detailed kinetic analysis, overview
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additional information
additional information
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Michaelis-Menten steady-state kinetic study. While Km ATP values increase with the ADP concentration, kcat values remain constant. The high affinity for the ADP product inhibitor considerably increases the estimated error for KmATP. Association and dissociation kinetics of flavin ligands to the RFK module are measured by flavin fluorescence changes, stopped-flow kinetics. Pre-steady-state kinetic analysis of the binding of flavins to the RFK module of CaFADS, thermodynamic diagram for the RFK-ligand interactions. Adenine and flavin nucleotide ligands cooperate in their binding to the RFK module. Detailed kinetic analysis, overview
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