| FMN adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.2 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a FMN adenylyltransferase ( EC 2.7.7.2) is an enzyme that catalyzes the chemical reaction
- ATP + FMN diphosphate + FAD
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 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
- 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.
| FMN adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.2 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a FMN adenylyltransferase ( EC 2.7.7.2) is an enzyme that catalyzes the chemical reaction
- ATP + FMN diphosphate + FAD
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 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
- 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.