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Literature summary for 2.7.7.2 extracted from

  • Krupa, A.; Sandhya, K.; Srinivasan, N.; Jonnalagadda, S.
    A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer (2003), Trends Biochem. Sci., 28, 9-12.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + FMN Corynebacterium ammoniagenes catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD diphosphate + FAD
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 r

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + FMN
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 Corynebacterium ammoniagenes diphosphate + FAD
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 r
ATP + FMN catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD Corynebacterium ammoniagenes diphosphate + FAD
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 r
ATP + riboflavin
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 Corynebacterium ammoniagenes ?
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 ?
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 ?
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