Biology:FAD-AMP lyase (cyclizing)
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FAD-AMP lyase (cyclizing) | |||||||||
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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 | ||||||||
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The enzyme FAD-AMP lyase (cyclizing) (EC 4.6.1.15) catalyzes the reaction
- FAD [math]\displaystyle{ \rightleftharpoons }[/math] 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
Further reading
- "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. March 1998. doi:10.1042/bj3300881. PMID 9480905.
- "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. November 2001. doi:10.1021/bi0157159. PMID 11695920.
Original source: https://en.wikipedia.org/wiki/FAD-AMP lyase (cyclizing).
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