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Literature summary extracted from

  • Efimov, I.; Kuusk, V.; Zhang, X.; McIntire, W.S.
    Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli (1998), Biochemistry, 37, 9716-9723.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.2 vector pET-23a(+) cloned and overexpressed in Escherichia coli JM109(DE-3) Corynebacterium ammoniagenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.2 diphosphate
-
 Corynebacterium ammoniagenes
2.7.7.2 FMN substrate inhibition Corynebacterium ammoniagenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.2 0.0004
-
 FAD pH 7.6, 25°C Corynebacterium ammoniagenes
2.7.7.2 0.001
-
 FMN pH 7.6, 25°C Corynebacterium ammoniagenes
2.7.7.2 0.037
-
 ATP pH 7.6, 25°C Corynebacterium ammoniagenes
2.7.7.2 0.114
-
 diphosphate pH 7.6, 25°C Corynebacterium ammoniagenes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.2 38000
-
-
 Corynebacterium ammoniagenes

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.2 ATP + FMN Corynebacterium ammoniagenes
-
 diphosphate + FAD
-
 r

Organism

EC Number Organism UniProt Comment Textmining
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.
2.7.7.2 ATP + FMN
-
 Corynebacterium ammoniagenes diphosphate + FAD
-
 r
2.7.7.2 ATP + FMN adenylation of FMN is reversible, FAD and diphosphate can be converted to FMN and ATP by the enzyme, under the conditions studied phosphorylation of riboflavin is irreversible Corynebacterium ammoniagenes diphosphate + FAD
-
 r
2.7.7.2 ATP + riboflavin
-
 Corynebacterium ammoniagenes ?
-
 ir
2.7.7.2 additional information bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26 Corynebacterium ammoniagenes ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.2 0.000075
-
 FAD pH 7.6, 25°C Corynebacterium ammoniagenes
2.7.7.2 0.0000833
-
 FMN pH 7.6, 25°C Corynebacterium ammoniagenes

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.2 0.00064
-
 diphosphate pH 7.6, 25°C Corynebacterium ammoniagenes
2.7.7.2 0.06
-
 diphosphate pH 7.6, 25°C Corynebacterium ammoniagenes