EC 2 - Transferases
EC 2.7 - Transferring phosphorus-containing groups
EC 2.7.7 - Nucleotidyltransferases
EC 2.7.7.2 - FAD synthetase
IntEnz Enzyme Nomenclature
EC 2.7.7.2
Names
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
Reaction
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17237 [IUBMB]ATPName origin: UniProt - CHECKED (C)Formula: C10H12N5O13P3
Charge: -4ChEBI compound status: CHECKED (C)FMNName origin: UniProt - CHECKED (C)Formula: C17H18N4O9P
Charge: -3ChEBI compound status: CHECKED (C)H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)=diphosphateName origin: UniProt - CHECKED (C)Formula: HO7P2
Charge: -3ChEBI compound status: CHECKED (C)
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
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]