|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 reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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 synθse, 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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