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Results: 2
Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): Preference for FAD andspecificity for splitting ribonucleoside diphosphate-X into ribonucleotideand a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion
Authors: Cabezas, A Pinto, RM Fraiz, F Canales, J Gonzalez-Santiago, S Cameselle, JC
Citation: A. Cabezas et al., Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): Preference for FAD andspecificity for splitting ribonucleoside diphosphate-X into ribonucleotideand a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion, BIOCHEM, 40(45), 2001, pp. 13710-13722
Preparation of riboflavin 4 ',5-cyclic phosphate by incubation of flavin-adenine dinucleotide with Mn2+ in the absence of riboflavin 5 '-phosphate cyclase
Authors: Pinto, RM Fraiz, FJ Cabezas, A Avalos, M Canales, J Costas, MJ Cameselle, JC
Citation: Rm. Pinto et al., Preparation of riboflavin 4 ',5-cyclic phosphate by incubation of flavin-adenine dinucleotide with Mn2+ in the absence of riboflavin 5 '-phosphate cyclase, ANALYT BIOC, 268(2), 1999, pp. 409-411
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