EC 2 - Transferases
EC 2.7 - Transferring phosphorus-containing groups
EC 2.7.7 - Nucleotidyltransferases
EC 2.7.7.2 - FAD synthase
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ENZYME view
IntEnz Enzyme Nomenclature
EC 2.7.7.2
Names
Accepted name:
FAD synthase
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
FAD synthetase [misleading]
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
FAD synthetase [misleading]
Systematic name:
ATP:FMN adenylyltransferase
Reaction
- ATP + FMN = diphosphate + FAD
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
Gene Ontology:
GO:0003919
CAS Registry Number:
9026-37-3
References
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Studies on flavinadenine dinucleotide-synthesizing enzyme in plants.Biochem. J. 75 : 381-386 (1960). [PMID: 13828163]
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Reversible enzymatic synthesis of flavin-adenine dinucleotide.J. Biol. Chem. 182 : 795-803 (1950).
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An FMN hydrolase is fused to a riboflavin kinase homolog in plants.J. Biol. Chem. 280 : 38337-38345 (2005). [PMID: 16183635]
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Complete purification and general characterization of FAD synthetase from rat liver.J. Biol. Chem. 262 : 7418-7422 (1987). [PMID: 3034893]
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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]