EC 2.7.7.2 - FAD synthetase

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IntEnz Enzyme Nomenclature
EC 2.7.7.2

Names

Accepted name:
FAD synthetase
Other names:
FAD pyrophosphorylase
FMN adenylyltransferase
adenosine triphosphate-riboflavin mononucleotide transadenylase
adenosine triphosphate-riboflavine mononucleotide transadenylase
riboflavin adenine dinucleotide pyrophosphorylase
riboflavin mononucleotide adenylyltransferase
riboflavine adenine dinucleotide adenylyltransferase
flavin adenine dinucleotide synthetase
FAD diphosphorylase
FADS
Systematic name:
ATP:FMN adenylyltransferase

Reaction

Cofactor

Comments:

Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [3]. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003919
CAS Registry Number: 9026-37-3
UniProtKB/Swiss-Prot: (87) [show] [UniProt]

References

  1. Giri, K.V., Rao, N.A., Cama, H.R. and Kumar, S.A.
    Studies on flavinadenine dinucleotide-synthesizing enzyme in plants.
    Biochem. J. 75: 381-386 (1960). [PMID: 13828163]
  2. Schrecker, A.W. and Kornberg, A.
    Reversible enzymatic synthesis of flavin-adenine dinucleotide.
    J. Biol. Chem. 182: 795-803 (1950).
  3. Sandoval, F.J. and Roje, S.
    An FMN hydrolase is fused to a riboflavin kinase homolog in plants.
    J. Biol. Chem. 280: 38337-38345 (2005). [PMID: 16183635]
  4. Oka, M. and McCormick, D.B.
    Complete purification and general characterization of FAD synthetase from rat liver.
    J. Biol. Chem. 262: 7418-7422 (1987). [PMID: 3034893]
  5. Brizio, C., Galluccio, M., Wait, R., Torchetti, E. M., Bafunno, V., Accardi, R., Gianazza, E., Indiveri, C., Barile, M.
    Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase.
    Biochem. Biophys. Res. Commun. 344: 1008-1016 (2006). [PMID: 16643857]

[EC 2.7.7.2 created 1961, modified 2007]