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Literature summary for 2.7.1.26 extracted from

  • Manstein, D.J.; Pai, E.F.
    Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes (1986), J. Biol. Chem., 261, 16169-16173.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
ATP ATP in form of MgATP2- Corynebacterium ammoniagenes

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ 38% of the activation with Zn2+ Corynebacterium ammoniagenes
Co2+ 34% of the activation with Zn2+ Corynebacterium ammoniagenes
Mg2+ 38% of the activation with Zn2+ Corynebacterium ammoniagenes
Mn2+ 31% of the activation with Zn2+ Corynebacterium ammoniagenes
Zn2+ best divalent metal activator Corynebacterium ammoniagenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
gel filtration Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
presence of ATP:riboflavin 5'-phosphotransferase and ATP:FMN adenylyltransferase on a single polypeptide Corynebacterium ammoniagenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-dATP + riboflavin
-
Corynebacterium ammoniagenes 2'-dADP + riboflavin 5'-phosphate
-
?
ATP + riboflavin
-
Corynebacterium ammoniagenes ADP + FMN
-
?

Subunits

Subunits Comment Organism
monomer 1 * 40000, SDS-PAGE Corynebacterium ammoniagenes