FAD-AMP lyase (cyclizing)

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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).

[edit] References

• IUBMB entry for 4.6.1.15
• BRENDA references for 4.6.1.15 (Recommended.)
• PubMed references for 4.6.1.15
• PubMed Central references for 4.6.1.15
• Google Scholar references for 4.6.1.15
• Cameselle JC (Pt 2). "Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver1". Biochem. J. 330: 881–8. PMID 9480905. 
• 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: 13710–22. doi:10.1021/bi0157159. PMID 11695920. 

[edit] External links

The CAS registry number for this enzyme class is 208349-48-8.

• IUBMB entry for 4.6.1.15

• KEGG entry for 4.6.1.15

• BRENDA entry for 4.6.1.15

• NiceZyme view of 4.6.1.15

• EC2PDB: PDB structures for 4.6.1.15

• PRIAM entry for 4.6.1.15

• PUMA2 entry for 4.6.1.15

• IntEnz: Integrated Enzyme entry for 4.6.1.15

• MetaCyc entry for 4.6.1.15

• Atomic-resolution structures of enzymes belonging to this class