FMN adenylyltransferase
In enzymology, a FMN adenylyltransferase (EC 2.7.7.2) is an enzyme that catalyzes the chemical reaction
- ATP + FMN diphosphate + FAD
FMN adenylyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 2.7.7.2 | ||||||||
CAS number | 9026-37-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
Thus, the two substrates of this enzyme are ATP and FMN, whereas its two products are diphosphate and FAD.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:FMN adenylyltransferase. This enzyme participates in riboflavin metabolism.
Other names
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
- riboflavine
gollark: Ridiculing people is cool and good™, censoring them isn't.
gollark: Power concentrated like that is *inherently* pretty bad because it could be misused at some point.
gollark: Suuuuuure.
gollark: If people believe things which cause them to make stupider decisions, too bad, they shouldn't do that.
gollark: Maybe with children, sure, as they can't really meaningfully decide very well.
References
- GIRI KV, RAO NA, CAMA HR, KUMAR SA (1960). "Studies on flavinadenine dinucleotide-synthesizing enzyme in plants". Biochem. J. 75: 381–6. PMC 1204435. PMID 13828163.
- Schrecker AW, Kornberg A (1950). "Reversible enzymatic synthesis of flavin-adenine dinucleotide". J. Biol. Chem. 182 (2): 795–803. PMID 19994476.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.