Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.26 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 2.7.1.26

Protein Variants

Protein Variants Comment Organism
E268A inactive Corynebacterium ammoniagenes
E268D the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
N210A inactive Corynebacterium ammoniagenes
N210D the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Corynebacterium ammoniagenes
T208A inactive Corynebacterium ammoniagenes
T208D inactive Corynebacterium ammoniagenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0021
-
 riboflavin apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
0.0041
-
 riboflavin apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
0.013
-
 riboflavin apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
0.0137
-
 ATP apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
0.0176
-
 ATP apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
0.0453
-
 ATP apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Turnover Number [1/s]

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

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.83
-
 ATP apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
3.83
-
 ATP apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
10.83
-
 riboflavin apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
40.3
-
 riboflavin apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
82.17
-
 ATP apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes
386
-
 riboflavin apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 Corynebacterium ammoniagenes