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Literature summary for 2.7.7.2 extracted from

  • Sebastian, M.; Serrano, A.; Velazquez-Campoy, A.; Medina, M.
    Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes (2017), Sci. Rep., 7, 7281 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.2

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Corynebacterium ammoniagenes
FMN
-
 Corynebacterium ammoniagenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 ATP pH 7.0, 25°C Corynebacterium ammoniagenes

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+ and the concerted fit of substrates are required to achieve a catalytically competent geometry 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
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.17
-
 FMN pH 7.0, 25°C Corynebacterium ammoniagenes

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0014
-
 FMN pH 7.0, 25°C Corynebacterium ammoniagenes
0.017
-
 ADP pH 7.0, 25°C Corynebacterium ammoniagenes

General Information

General Information Comment Organism
physiological function in a truncated FADS variant consisting in the isolated C-terminal ATP:riboflavin kinase RFK module, RFK activity is similar to that of the full-length enzyme. Inhibition of the RFK activity by the RF substrate is independent of the FMN:ATP adenylyltransferase module, and FMN production, in addition to being inhibited by an excess of riboflavin, is also inhibited by both of the reaction products. Mg2+ and the concerted fit of substrates are required to achieve a catalytically competent geometry Corynebacterium ammoniagenes