|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
Enzymes and Genes:
bifunctional riboflavin kinase / FMN adenylyltransferase: ribF
In Pathway: flavin biosynthesis I (bacteria and plants)
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: FAD synthetase
Enzyme Commission Synonyms: FAD pyrophosphorylase, riboflavin mononucleotide adenylyltransferase, adenosine triphosphate-riboflavin mononucleotide transadenylase, adenosine triphosphate-riboflavine mononucleotide transadenylase, riboflavin adenine dinucleotide pyrophosphorylase, riboflavine adenine dinucleotide adenylyltransferase, flavin adenine dinucleotide synthetase, FADS, FMN adenylyltransferase
This reaction produces FAD from FMN.
Enzyme Commission Summary:
Requires Mg2+ and is highly specific for ATP as phosphate donor [Brizio06]. 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 [Sandoval05]. 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 126.96.36.199, riboflavin kinase [Sandoval05, Brizio06].
Brizio06: Brizio C, Galluccio M, Wait R, Torchetti EM, Bafunno V, Accardi R, Gianazza E, Indiveri C, Barile M (2006). "Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase." Biochem Biophys Res Commun 344(3);1008-16. PMID: 16643857
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