FMN adenylyltransferase
| FMN adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.2 | ||||||||
| CAS no. | 9026-37-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
FMN adenylyltransferase (EC 2.7.7.2) is an enzyme that catalyzes the reversible chemical reaction that produces flavin adenine dinucleotide from adenosine triphosphate and flavin mononucleotide (FMN).
Function
Flavin adenine dinucleotide, is a coenzyme found in all organisms.[1] It is produced by FMN adenylyltransferase, which combines adenosine triphosphate and flavin mononucleotide, with inorganic pyrophosphate (PPi) produced as a byproduct:
The enzyme has been characterised from yeast, plants and humans.[2][3][4][5]
Nomenclature
The enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:FMN adenylyltransferase. Other names in common use include
- FAD pyrophosphorylase
- riboflavin mononucleotide adenylyltransferase
- adenosine triphosphate-riboflavin mononucleotide transadenylase
- adenosine triphosphate-riboflavine mononucleotide transadenylase
- FAD synthetase
- riboflavin adenine dinucleotide pyrophosphorylase[6]
References
- ↑ Hayashi, Hideyuki (2013). B Vitamins and Folate: Chemistry, Analysis, Function and Effects. Cambridge, UK: The Royal Society of Chemistry. ISBN 978-1-84973-369-4.
- ↑ Schrecker, Anthony W.; Kornberg, Arthur. (1950). "Reversible Enzymatic Synthesis of Flavin-Adenine Dinucleotide". Journal of Biological Chemistry. 182 (2): 795–803. doi:10.1016/S0021-9258(18)56514-5. PMID 19994476.
- ↑ Giri, K. V.; Rao, N. Appaji; Cama, H. R.; Kumar, S. A. (1960). "Studies on flavinadenine dinucleotide-synthesizing enzyme in plants". Biochemical Journal. 75 (2): 381–386. doi:10.1042/bj0750381. PMC 1204435. PMID 13828163.
- ↑ Sandoval, Francisco J.; Roje, Sanja (2005). "An FMN Hydrolase is Fused to a Riboflavin Kinase Homolog in Plants". Journal of Biological Chemistry. 280 (46): 38337–38345. doi:10.1074/jbc.M500350200. PMID 16183635.
- ↑ Brizio, Carmen; Galluccio, Michele; Wait, Robin; et al. (2006). "Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase". Biochemical and Biophysical Research Communications. 344 (3): 1008–1016. doi:10.1016/j.bbrc.2006.04.003. PMID 16643857.
- ↑ Enzyme 2.7.7.2 at KEGG Pathway Database.
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