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Literature summary for 2.7.7.2 extracted from

  • Herguedas, B.; Martinez-Julvez, M.; Frago, S.; Medina, M.; Hermoso, J.A.
    Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes (2010), J. Mol. Biol., 400, 218-230.
    View publication on PubMed
Search for more literature for 2.7.7.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0054
-
 FMN FADS monomer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
0.0311
-
 FMN FADS trimer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
0.0435
-
 ATP FADS trimer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
0.079
-
 ATP FADS monomer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
phenyl Sepharose column chromatography and DEAE-cellulose column chromatography Corynebacterium ammoniagenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + FMN
-
 Corynebacterium ammoniagenes diphosphate + FAD
-
 r
diphosphate + FAD
-
 Corynebacterium ammoniagenes ATP + FMN
-
 r
additional information FAD synthetase presents two catalytic modules, a C-terminus with ATP-riboflavin kinase activity and an N-terminus with ATP-flavin mononucleotide adenylyltransferase activity Corynebacterium ammoniagenes ?
-
 ?

Subunits

Subunits Comment Organism
hexamer x-ray crystallography Corynebacterium ammoniagenes

Synonyms

Synonyms Comment Organism
ATP-FMN adenylyltransferase
-
 Corynebacterium ammoniagenes
FADS
-
 Corynebacterium ammoniagenes
FMNAT
-
 Corynebacterium ammoniagenes

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.047
-
 FMN FADS trimer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
0.33
-
 FMN FADS monomer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), 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
0.0311
-
 FMN FADS trimer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
1.1
-
 ATP FADS trimer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
4.2
-
 ATP FADS monomer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes
61.7
-
 FMN FADS monomer, 10 mM MgCl2 in 50 mM Tris–HCl (pH 8.0), at 37°C Corynebacterium ammoniagenes