Agosin M, Ankley G T
Drug Metab Dispos. 1987 Mar-Apr;15(2):200-3.
A cytosolic NADPH-dependent FAD-containing enzyme purified from Trypanosoma cruzi epimastigotes [Kuwahara, White, and Agosin: Biochem. Biophys. Res. Commun. 124, 121 (1984); Arch. Biochem. Biophys. 239, 18 (1985)] catalyzes the conversion of N,N-dimethylaniline to its corresponding N-oxide. The identity of the product has been established by high performance liquid chromatography and paper chromatography elution patterns and by electron impact spectrometry. The oxidation of N,N-dimethylaniline was determined by following the oxidation of NADPH spectrophotometrically, and a double reciprocal plot of reaction velocity vs. substrate concentration was prepared. At an optimum pH of 8.0, the plot resulted in Km and Vmax values of 56 microM and 114 nmol X min-1 X mg of protein-1, respectively. The oxidative activity of the enzyme suggests that it may be involved in detoxication processes which may contribute to the resistance of T. cruzi to known antiprotozoal drugs.
从克氏锥虫前鞭毛体中纯化得到的一种胞质型依赖烟酰胺腺嘌呤二核苷酸磷酸（NADPH）且含有黄素腺嘌呤二核苷酸（FAD）的酶[桑原、怀特和阿戈辛：《生物化学与生物物理学研究通讯》124, 121 (1984)；《生物化学与生物物理学档案》239, 18 (1985)]催化N,N - 二甲基苯胺转化为其相应的N - 氧化物。产物的身份已通过高效液相色谱法、纸色谱洗脱图谱以及电子轰击光谱法得以确定。通过分光光度法跟踪NADPH的氧化来测定N,N - 二甲基苯胺的氧化情况，并制备了反应速度与底物浓度的双倒数图。在最适pH值为8.0时，该图得出的米氏常数（Km）和最大反应速度（Vmax）值分别为56微摩尔和114纳摩尔×分钟⁻¹×毫克蛋白质⁻¹。该酶的氧化活性表明它可能参与解毒过程，这可能有助于克氏锥虫对已知抗寄生虫药物产生抗性。
