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Literature summary extracted from

  • Serrano, A.; Frago, S.; Velazquez-Campoy, A.; Medina, M.
    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 (2012), Int. J. Mol. Sci., 13, 14492-14517.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.26 H28A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 H28D the mutant shows reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 H31A the mutant shows increased catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 N125A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 N125D the mutant shows reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 R161A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 R161D the mutant shows wild type catalytic efficiency Corynebacterium ammoniagenes
2.7.1.26 S164A the mutant shows increased catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 S164D the mutant shows increased catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 T165A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 T165D the mutant shows wild type catalytic efficiency Corynebacterium ammoniagenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.26 riboflavin substrate inhibition Corynebacterium ammoniagenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.26 0.0017
-
 riboflavin mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0045
-
 riboflavin mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0056
-
 riboflavin mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0077
-
 riboflavin mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0088
-
 riboflavin mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.01
-
 ATP mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.01
-
 riboflavin mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.011
-
 ATP mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.011
-
 ATP mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.012
-
 ATP mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.012
-
 ATP mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.012
-
 riboflavin mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.012
-
 ATP mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.012
-
 ATP mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.013
-
 riboflavin mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.013
-
 riboflavin wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.014
-
 ATP mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.014
-
 ATP mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.014
-
 ATP wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.016
-
 riboflavin mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.023
-
 riboflavin mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.024
-
 ATP mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.025
-
 riboflavin mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.035
-
 ATP mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.26 Corynebacterium ammoniagenes Q59263
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.26 ATP + riboflavin
-
 Corynebacterium ammoniagenes ADP + FMN
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.26 ATP:riboflavin kinase
-
 Corynebacterium ammoniagenes
2.7.1.26 FAD synthetase bifunctional enzyme, the C-terminal is associated with ATP:riboflavin kinase activity and the N-terminal associated with ATP:FMN adenylyltransferase activity Corynebacterium ammoniagenes
2.7.1.26 FADS
-
 Corynebacterium ammoniagenes
2.7.1.26 RFK
-
 Corynebacterium ammoniagenes

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.26 0.75
-
 ATP mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.75
-
 ATP mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.77
-
 ATP mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.92
-
 ATP mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.92
-
 ATP mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.97
-
 ATP mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.98
-
 ATP mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1.08
-
 ATP mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1.1
-
 ATP mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1.13
-
 ATP mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1.13
-
 ATP wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1.33
-
 ATP mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1.85
-
 riboflavin mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 2.82
-
 riboflavin mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 2.85
-
 riboflavin mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 3
-
 riboflavin mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 3.08
-
 riboflavin mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 4.32
-
 riboflavin mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 4.78
-
 riboflavin mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 5
-
 riboflavin mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 5
-
 riboflavin mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 5.02
-
 riboflavin wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 6.92
-
 riboflavin mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 7.12
-
 riboflavin mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.26 0.0018
-
 riboflavin mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0019
-
 riboflavin mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0032
-
 riboflavin mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0033
-
 riboflavin mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.004
-
 riboflavin wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0041
-
 riboflavin mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0044
-
 riboflavin mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0046
-
 riboflavin mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0051
-
 riboflavin mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0051
-
 riboflavin mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0058
-
 riboflavin mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 0.0063
-
 riboflavin mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.26 31.7
-
 ATP mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 38.3
-
 ATP mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 51.7
-
 ATP mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 68.3
-
 ATP mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 71.7
-
 ATP mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 78.3
-
 ATP mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 81.7
-
 ATP wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 83.3
-
 ATP mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 88.3
-
 ATP mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 90
-
 ATP mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 93.3
-
 ATP mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 101.7
-
 ATP mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 200
-
 riboflavin mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 283
-
 riboflavin mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 300
-
 riboflavin mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 383
-
 riboflavin mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 383
-
 riboflavin mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 383
-
 riboflavin wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 417
-
 riboflavin mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 433
-
 riboflavin mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 483
-
 riboflavin mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 550
-
 riboflavin mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 617
-
 riboflavin mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes
2.7.1.26 1083
-
 riboflavin mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C Corynebacterium ammoniagenes