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Literature summary for 2.7.7.2 extracted from

  • Serrano, A.; Arilla-Luna, S.; Medina, M.
    Insights into the fmnat active site of FAD synthase Aromaticity is essential for flavin binding and catalysis (2020), Int. J. Mol. Sci., 21, 3738 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.2

Protein Variants

Protein Variants Comment Organism
F128A loss of NMNAT activity Corynebacterium ammoniagenes
F128K loss of NMNAT activity Corynebacterium ammoniagenes
F128W mutant retains NMNAT activity Corynebacterium ammoniagenes
F62A loss of NMNAT activity Corynebacterium ammoniagenes
F62K loss of NMNAT activity Corynebacterium ammoniagenes
F62W mutant retains NMNAT activity Corynebacterium ammoniagenes
Y106A loss of NMNAT activity Corynebacterium ammoniagenes
Y106K loss of NMNAT activity Corynebacterium ammoniagenes
Y106W mutant retains NMNAT activity Corynebacterium ammoniagenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
 FMN wild-type, pH 7.0, 25°C Corynebacterium ammoniagenes
0.009
-
 ATP mutant F128W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.012
-
 FMN mutant Y106W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.019
-
 ATP mutant Y106W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.042
-
 FMN mutant F62W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.043
-
 ATP wild-type, pH 7.0, 25°C Corynebacterium ammoniagenes
0.051
-
 ATP mutant F62W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.108
-
 FMN mutant F128W, pH 7.0, 25°C Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes Q59263 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
0.43
-
 FMN mutant F128W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.48
-
 FMN mutant F62W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.6
-
 FMN mutant Y106W, pH 7.0, 25°C Corynebacterium ammoniagenes
0.65
-
 FMN wild-type, pH 7.0, 25°C Corynebacterium ammoniagenes

General Information

General Information Comment Organism
physiological function distortion of aromaticity at the FMNAT isoalloxazine binding cavity prevents FMN and FAD from correct accommodation in their binding cavity and decreases the efficiency of the FMNAT activity. The side-chains of F62, Y106 and F128 are relevant in the formation of the catalytic competent complex during FMNAT catalysis in bifunctional FAD synthase Corynebacterium ammoniagenes

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3
-
 FMN mutant F128W, pH 7.0, 25°C Corynebacterium ammoniagenes
10
-
 ATP mutant F62W, pH 7.0, 25°C Corynebacterium ammoniagenes
12
-
 FMN mutant F62W, pH 7.0, 25°C Corynebacterium ammoniagenes
15
-
 ATP wild-type, pH 7.0, 25°C Corynebacterium ammoniagenes
38
-
 ATP mutant Y106W, pH 7.0, 25°C Corynebacterium ammoniagenes
48
-
 ATP mutant F128W, pH 7.0, 25°C Corynebacterium ammoniagenes
60
-
 FMN mutant Y106W, pH 7.0, 25°C Corynebacterium ammoniagenes
100
-
 FMN wild-type, pH 7.0, 25°C Corynebacterium ammoniagenes