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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.2 expressed in Escherichia coli Corynebacterium ammoniagenes

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.26 E268A inactive Corynebacterium ammoniagenes
2.7.1.26 E268D the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 N210A inactive Corynebacterium ammoniagenes
2.7.1.26 N210D the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.1.26 T208A inactive Corynebacterium ammoniagenes
2.7.1.26 T208D inactive Corynebacterium ammoniagenes
2.7.7.2 E268A the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.7.2 E268D the mutant shows about wild type catalytic efficiencies for ATP and FMN Corynebacterium ammoniagenes
2.7.7.2 N210A the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.7.2 N210D the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.7.2 T208A the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme Corynebacterium ammoniagenes
2.7.7.2 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.26 0.0021
-
riboflavin apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.0041
-
riboflavin apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.013
-
riboflavin apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.0137
-
ATP apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.0176
-
ATP apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.0453
-
ATP apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.00088
-
FMN mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.00088
-
FMN mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.00095
-
FMN mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.00117
-
FMN mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.00119
-
FMN wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.00823
-
FMN mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.01501
-
FMN mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.03568
-
ATP wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.0382
-
ATP mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.0387
-
ATP mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.04537
-
ATP mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.04647
-
ATP mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.04704
-
ATP mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 0.07667
-
ATP mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.26 Corynebacterium ammoniagenes
-
-
-
2.7.7.2 Corynebacterium ammoniagenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.2
-
Corynebacterium ammoniagenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.26 ATP + riboflavin
-
Corynebacterium ammoniagenes ADP + FMN
-
?
2.7.7.2 ATP + FMN
-
Corynebacterium ammoniagenes diphosphate + FAD
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.26 ATP: riboflavin kinase
-
Corynebacterium ammoniagenes
2.7.1.26 RFK
-
Corynebacterium ammoniagenes
2.7.1.26 riboflavin kinase/FMN adenylyltransferase FADS, bifunctional enzyme, the C-terminus exhibits ATP: riboflavin kinase activity Corynebacterium ammoniagenes
2.7.7.2 ATP:FMN adenylyltransferase
-
Corynebacterium ammoniagenes
2.7.7.2 FADS
-
Corynebacterium ammoniagenes
2.7.7.2 FMNAT
-
Corynebacterium ammoniagenes

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.26 0.042
-
ATP apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.045
-
riboflavin apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.07
-
ATP apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 0.085
-
riboflavin apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 1.13
-
ATP apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 5
-
riboflavin apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.26 0.83
-
ATP apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 3.83
-
ATP apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 10.83
-
riboflavin apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 40.3
-
riboflavin apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 82.17
-
ATP apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.1.26 386
-
riboflavin apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 3.8
-
ATP mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 4.3
-
ATP mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 7.3
-
ATP mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 7.7
-
ATP mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 8
-
ATP wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 8.2
-
ATP mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 8.5
-
ATP mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 19.7
-
FMN mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 24.8
-
FMN mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 238.3
-
FMN wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 270.2
-
FMN mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 365.7
-
FMN mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 369.2
-
FMN mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes
2.7.7.2 386
-
FMN mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2 Corynebacterium ammoniagenes