Fraiz F J, Pinto R M, Costas M J, Aavalos M, Canales J, Cabezas A, Cameselle J C
Unidad de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad de Extremadura, Apartado 108, E-06080 Badajoz, Spain.
Biochem J. 1998 Mar 1;330 ( Pt 2)(Pt 2):881-8. doi: 10.1042/bj3300881.
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.
从大鼠肝脏匀浆的胞质部分中部分纯化出一种酶活性,该酶可将黄素腺嘌呤二核苷酸(FAD)分解为腺苷酸(AMP)和核黄素4',5'-环磷酸酯(4',5'-cFMN),其米氏常数(Km)为6 - 8微摩尔。通过酶分析、高效液相色谱(HPLC)、紫外可见光谱和核磁共振(NMR)光谱分析对4',5'-cFMN进行了表征。数据表明,涉及一种新酶,暂命名为FAD - AMP裂解酶(环化)或FMN环化酶。此外,大鼠肝脏环磷酸二酯酶可将4',5'-cFMN水解为5'-FMN。结果表明哺乳动物体内黄素存在一种新的酶促途径,并支持4',5'-cFMN的生物学相关性,其可能作为黄素辅酶或调节信号。