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Metabolic Modeling Tutorial
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Escherichia coli K-12 substr. MG1655 Reaction: 2.7.7.2

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.7.2

Enzymes and Genes:
bifunctional riboflavin kinase / FMN adenylyltransferase Inferred from experiment : 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

Summary:
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 2.7.1.26, riboflavin kinase [Sandoval05, Brizio06].

Citations: [GIRI60, Oka87]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.7.7.2 , ENZYME:EC:2.7.7.2 , IUBMB-ExplorEnz:EC:2.7.7.2


References

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


Report Errors or Provide Feedback
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 18.5 on Thu Nov 27, 2014, biocyc11.