The Enzyme Database

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Accepted name: FAD-AMP lyase (cyclizing)
Reaction: FAD = AMP + riboflavin cyclic-4′,5′-phosphate
Other name(s): FMN cyclase; FAD AMP-lyase (cyclic-FMN-forming)
Systematic name: FAD AMP-lyase (riboflavin-cyclic-4′,5′-phosphate-forming)
Comments: Requires Mn2+ or Co2+. While FAD was the best substrate tested [2], the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 208349-48-8
1.  Fraiz, F.J., Pinto, R.M., Costas, M.J., Avalos, M., Canales, J., Cabezas, A. and Cameselle, J.C. Enzymic formation of riboflavin 4′,5′-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver. Biochem. J. 330 (1998) 881–888. [PMID: 9480905]
2.  Cabezas, A., Pinto, R.M., Fraiz, F., Canales, J., Gonzalez-Santiago, S. and Cameselle, J.C. 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 (2001) 13710–13722. [DOI] [PMID: 11695920]
[EC created 2002]

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