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Literature summary for 2.7.7.2 extracted from

  • Serrano, A.; Frago, S.; Herguedas, B.; Martinez-Julvez, M.; Velazquez-Campoy, A.; Medina, M.
    Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes (2013), Cell Biochem. Biophys., 65, 57-68.
    View publication on PubMed
Search for more literature for 2.7.7.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Corynebacterium ammoniagenes

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme E268D, hanging drop vapor diffusion method Corynebacterium ammoniagenes

Protein Variants

Protein Variants Comment Organism
E268A the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme Corynebacterium ammoniagenes
E268D the mutant shows about wild type catalytic efficiencies for ATP and FMN Corynebacterium ammoniagenes
N210A the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme Corynebacterium ammoniagenes
N210D the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme Corynebacterium ammoniagenes
T208A the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme Corynebacterium ammoniagenes
T208D the mutant shows increased catalytic efficiency for FMN and increased catalytic efficiency for ATP compared to the wild type enzyme Corynebacterium ammoniagenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00088
-
 FMN mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.00088
-
 FMN mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.00095
-
 FMN mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.00117
-
 FMN mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.00119
-
 FMN wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.00823
-
 FMN mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.01501
-
 FMN mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.03568
-
 ATP wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.0382
-
 ATP mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.0387
-
 ATP mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.04537
-
 ATP mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.04647
-
 ATP mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.04704
-
 ATP mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
0.07667
-
 ATP mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium ammoniagenes

Substrates and Products (Substrate)

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

Synonyms

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.8
-
 ATP mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
4.3
-
 ATP mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
7.3
-
 ATP mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
7.7
-
 ATP mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
8
-
 ATP wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
8.2
-
 ATP mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
8.5
-
 ATP mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
19.7
-
 FMN mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
24.8
-
 FMN mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
238.3
-
 FMN wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
270.2
-
 FMN mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
365.7
-
 FMN mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
369.2
-
 FMN mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
386
-
 FMN mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes