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Literature summary for 2.7.1.26 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

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

Inhibitors

Inhibitors Comment Organism Structure
riboflavin substrate inhibition Corynebacterium ammoniagenes

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes Q59263
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ATP:riboflavin kinase
-
Corynebacterium ammoniagenes
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
FADS
-
Corynebacterium ammoniagenes
RFK
-
Corynebacterium ammoniagenes

Turnover Number [1/s]

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

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

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