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Literature summary for 2.7.7.2 extracted from

  • Serrano, A.; Sebastian, M.; Arilla-Luna, S.; Baquedano, S.; Herguedas, B.; Velazquez-Campoy, A.; Martinez-Julvez, M.; Medina, M.
    The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes (2017), Sci. Rep., 7, 404 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.2

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure predicts a dimer of trimers organization Corynebacterium ammoniagenes

Protein Variants

Protein Variants Comment Organism
D298A mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
D298E mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
E203A mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
E301A mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
E301K mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
F206A mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
F206K mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
F206W mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
K202A mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
L304K mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
V300A mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes
V300K mutation at the macromolecular interface between two protomers within the trimer Corynebacterium ammoniagenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00042
-
 FMN mutant E301A, pH 7, 25°C Corynebacterium ammoniagenes
0.0007
-
 FMN mutant E203A, pH 7, 25°C Corynebacterium ammoniagenes
0.00085
-
 FMN mutant E301K, pH 7, 25°C Corynebacterium ammoniagenes
0.00095
-
 FMN mutant D298E, pH 7, 25°C Corynebacterium ammoniagenes
0.0012
-
 FMN mutant D298A, pH 7, 25°C Corynebacterium ammoniagenes
0.0014
-
 FMN mutant V300A, pH 7, 25°C Corynebacterium ammoniagenes
0.0017
-
 FMN mutant F206W, pH 7, 25°C Corynebacterium ammoniagenes
0.0028
-
 FMN mutant EL04A, pH 7, 25°C Corynebacterium ammoniagenes
0.0029
-
 FMN mutant F206A, pH 7, 25°C Corynebacterium ammoniagenes
0.0029
-
 FMN mutant K202A, pH 7, 25°C Corynebacterium ammoniagenes
0.0054
-
 FMN mutant F206K, pH 7, 25°C Corynebacterium ammoniagenes
0.0083
-
 FMN mutant V300K, pH 7, 25°C Corynebacterium ammoniagenes
0.0095
-
 ATP mutant V300K, pH 7, 25°C Corynebacterium ammoniagenes
0.0101
-
 FMN wild-type, pH 7, 25°C Corynebacterium ammoniagenes
0.0104
-
 ATP mutant D298E, pH 7, 25°C Corynebacterium ammoniagenes
0.0108
-
 ATP mutant E203A, pH 7, 25°C Corynebacterium ammoniagenes
0.0115
-
 ATP mutant L304K, pH 7, 25°C Corynebacterium ammoniagenes
0.0121
-
 ATP mutant K202A, pH 7, 25°C Corynebacterium ammoniagenes
0.0152
-
 FMN mutant L304K, pH 7, 25°C Corynebacterium ammoniagenes
0.0153
-
 ATP mutant E301K, pH 7, 25°C Corynebacterium ammoniagenes
0.0197
-
 ATP mutant E301A, pH 7, 25°C Corynebacterium ammoniagenes
0.0207
-
 ATP mutant D298A, pH 7, 25°C Corynebacterium ammoniagenes
0.0224
-
 ATP wild-type, pH 7, 25°C Corynebacterium ammoniagenes
0.0252
-
 ATP mutant F206W, pH 7, 25°C Corynebacterium ammoniagenes
0.0347
-
 ATP mutant EL04A, pH 7, 25°C Corynebacterium ammoniagenes
0.038
-
 ATP mutant F206A, pH 7, 25°C Corynebacterium ammoniagenes
0.0388
-
 ATP mutant F206K, pH 7, 25°C Corynebacterium ammoniagenes
0.0462
-
 ATP mutant V300A, pH 7, 25°C Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes Q59263 bifunctional riboflavin kinase/FMN adenylyltransferase, cf. EC 2.7.1.26
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ribF
-
 Corynebacterium ammoniagenes

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.038
-
 FMN mutant K202A, pH 7, 25°C Corynebacterium ammoniagenes
0.042
-
 FMN mutant EL04A, pH 7, 25°C Corynebacterium ammoniagenes
0.053
-
 FMN mutant E203A, pH 7, 25°C Corynebacterium ammoniagenes
0.055
-
 FMN mutant D298E, pH 7, 25°C Corynebacterium ammoniagenes
0.07
-
 FMN mutant F206A, pH 7, 25°C Corynebacterium ammoniagenes
0.077
-
 FMN mutant F206W, pH 7, 25°C Corynebacterium ammoniagenes
0.077
-
 FMN mutant V300K, pH 7, 25°C Corynebacterium ammoniagenes
0.082
-
 FMN mutant V300A, pH 7, 25°C Corynebacterium ammoniagenes
0.087
-
 FMN mutant L304K, pH 7, 25°C Corynebacterium ammoniagenes
0.091
-
 FMN wild-type, pH 7, 25°C Corynebacterium ammoniagenes
0.101
-
 FMN mutant D298A, pH 7, 25°C Corynebacterium ammoniagenes
0.103
-
 FMN mutant F206K, pH 7, 25°C Corynebacterium ammoniagenes
0.105
-
 FMN mutant E301K, pH 7, 25°C Corynebacterium ammoniagenes
0.115
-
 FMN mutant E301A, pH 7, 25°C Corynebacterium ammoniagenes

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.17
-
 ATP mutant EL04A, pH 7, 25°C Corynebacterium ammoniagenes
1.83
-
 ATP mutant V300A, pH 7, 25°C Corynebacterium ammoniagenes
1.833
-
 ATP mutant F206A, pH 7, 25°C Corynebacterium ammoniagenes
2.67
-
 ATP mutant F206K, pH 7, 25°C Corynebacterium ammoniagenes
3.17
-
 ATP mutant K202A, pH 7, 25°C Corynebacterium ammoniagenes
3.67
-
 ATP mutant F206W, pH 7, 25°C Corynebacterium ammoniagenes
4.17
-
 ATP wild-type, pH 7, 25°C Corynebacterium ammoniagenes
5
-
 ATP mutant D298A, pH 7, 25°C Corynebacterium ammoniagenes
5
-
 ATP mutant E203A, pH 7, 25°C Corynebacterium ammoniagenes
5.17
-
 ATP mutant D298E, pH 7, 25°C Corynebacterium ammoniagenes
5.83
-
 ATP mutant E301A, pH 7, 25°C Corynebacterium ammoniagenes
6.83
-
 ATP mutant E301K, pH 7, 25°C Corynebacterium ammoniagenes
7.5
-
 ATP mutant L304K, pH 7, 25°C Corynebacterium ammoniagenes
8
-
 ATP mutant V300K, pH 7, 25°C Corynebacterium ammoniagenes
9
-
 FMN wild-type, pH 7, 25°C Corynebacterium ammoniagenes
9.17
-
 FMN mutant V300K, pH 7, 25°C Corynebacterium ammoniagenes
13.33
-
 FMN mutant K202A, pH 7, 25°C Corynebacterium ammoniagenes
15.17
-
 FMN mutant EL04A, pH 7, 25°C Corynebacterium ammoniagenes
19.17
-
 FMN mutant F206K, pH 7, 25°C Corynebacterium ammoniagenes
24.17
-
 FMN mutant F206A, pH 7, 25°C Corynebacterium ammoniagenes
55
-
 FMN mutant F206W, pH 7, 25°C Corynebacterium ammoniagenes
56.67
-
 FMN mutant L304K, pH 7, 25°C Corynebacterium ammoniagenes
57.83
-
 FMN mutant D298E, pH 7, 25°C Corynebacterium ammoniagenes
58.33
-
 FMN mutant V300A, pH 7, 25°C Corynebacterium ammoniagenes
75
-
 FMN mutant E203A, pH 7, 25°C Corynebacterium ammoniagenes
85
-
 FMN mutant D298A, pH 7, 25°C Corynebacterium ammoniagenes
123.33
-
 FMN mutant E301K, pH 7, 25°C Corynebacterium ammoniagenes
273.33
-
 FMN mutant E301A, pH 7, 25°C Corynebacterium ammoniagenes