FAD-AMP lyase (cyclizing)
| FAD-AMP lyase (cyclizing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.6.1.15 | ||||||||
| CAS number | 208349-48-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a FAD-AMP lyase (cyclizing) (EC 4.6.1.15) is an enzyme that catalyzes the chemical reaction
- FAD AMP + riboflavin cyclic-4',5'-phosphate
Hence, this enzyme has one substrate, FAD, and two products, AMP and riboflavin cyclic-4',5'-phosphate.
This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is FAD AMP-lyase (riboflavin-cyclic-4',5'-phosphate-forming). Other names in common use include FMN cyclase, and FAD AMP-lyase (cyclic-FMN-forming).
References
- Cameselle JC; Pinto, RM; Costas, MJ; Aavalos, M; Canales, J; Cabezas, A; Cameselle, JC (1998). "Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver1". Biochem. J. 330 (Pt 2): 881–8. PMC 1219220
. PMID 9480905. - Cameselle JC; Pinto, RM; Fraiz, F; Canales, J; González-Santiago, S; Cameselle, JC (2001). "Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion". Biochemistry. 40 (45): 13710–22. doi:10.1021/bi0157159. PMID 11695920.
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