| Literature DB >> 9480905 |
F J Fraiz1, R M Pinto, M J Costas, M Aavalos, J Canales, A Cabezas, J C Cameselle.
Abstract
An enzyme activity splitting FAD to AMP and riboflavin 4',5'-cyclic phosphate (4',5'-cFMN), with a Km of 6-8 microM, was partially purified from the cytosolic fraction of rat liver homogenates. 4', 5'-cFMN was characterized by enzyme, HPLC, UV-visible and NMR spectroscopic analyses. The data suggest that a novel enzyme, tentatively named FAD-AMP lyase (cyclizing) or FMN cyclase, is involved. Also, 4',5'-cFMN was hydrolysed to 5'-FMN by a rat liver cyclic phosphodiesterase. The results indicate a novel enzymic pathway for flavins in mammals, and support the biological relevance of 4',5'-cFMN, perhaps as a flavocoenzyme or a regulatory signal.Entities:
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Year: 1998 PMID： 9480905 PMCID： PMC1219220 DOI： 10.1042/bj3300881
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857