The enzyme FAD-AMP lyase (cyclizing) (EC 4.6.1.15) catalyzes the reaction
| FAD-AMP lyase (cyclizing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.6.1.15 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
- FAD AMP + 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
editFurther reading
edit- Fraiz FJ, Pinto RM, Costas MJ, Aavalos M, Canales J, Cabezas A, Cameselle JC (March 1998). "Enzymic formation of riboflavin 4′,5′-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver". The Biochemical Journal. 330 ( Pt 2) (Pt 2): 881–8. doi:10.1042/bj3300881. PMC 1219220. PMID 9480905.
- Cabezas A, Pinto RM, Fraiz F, Canales J, González-Santiago S, Cameselle JC (November 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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