Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:
bifunctional riboflavin kinase / FMN adenylyltransferaseInferred from experiment: 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, riboflavin kinase [Sandoval05, Brizio06].

Citations: [GIRI60, Oka87]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


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

GIRI60: GIRI KV, RAO NA, CAMA HR, KUMAR SA (1960). "Studies on flavinadenine dinucleotide-synthesizing enzyme in plants." Biochem J 75;381-6. PMID: 13828163

Oka87: Oka M, McCormick DB (1987). "Complete purification and general characterization of FAD synthetase from rat liver." J Biol Chem 262(15);7418-22. PMID: 3034893

Sandoval05: Sandoval FJ, Roje S (2005). "An FMN hydrolase is fused to a riboflavin kinase homolog in plants." J Biol Chem 280(46);38337-45. PMID: 16183635

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.5 on Thu Nov 26, 2015, BIOCYC13A.