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Literature summary for 2.7.7.2 extracted from

  • Mack, M.; van Loon, A.P.; Hohmann, H.P.
    Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC (1998), J. Bacteriol., 180, 950-955.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
ribC encodes a bifunctional flavokinase/FAD-synthetase, cloned and overexpressed in Escherichia coli BL21 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34180
-
wild-type, gel filtration Bacillus subtilis
34200
-
gel filtration, nondenaturing conditions Bacillus subtilis
34230
-
mutant RibC, gel filtration Bacillus subtilis
35670
-
mass spectroscopy Bacillus subtilis
35670
-
deduced from RibC open reading frame Bacillus subtilis
36000
-
wild-type, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + FMN Bacillus subtilis essential for flavin metabolism diphosphate + FAD
-
r

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P54575 1012
-
Bacillus subtilis 168 P54575 1012
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and recombinant enzyme Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.58
-
-
Bacillus subtilis

Storage Stability

Storage Stability Organism
-20°C, stable for at least 2 weeks Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + FMN
-
Bacillus subtilis diphosphate + FAD
-
r
ATP + FMN essential for flavin metabolism Bacillus subtilis diphosphate + FAD
-
r
additional information bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26 Bacillus subtilis ?
-
?
additional information highly purified 5'-FMN is not accepted as a substrate Bacillus subtilis ?
-
?
additional information bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26 Bacillus subtilis 168 ?
-
?
additional information highly purified 5'-FMN is not accepted as a substrate Bacillus subtilis 168 ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 36000, SDS-PAGE Bacillus subtilis