Axarli Irene, Prigipaki Ariadne, Labrou Nikolaos E
Laboratory of Enzyme Technology, Department of Agricultural Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece.
Enzyme Res. 2010 Jul 1;2010:125429. doi: 10.4061/2010/125429.
Bacterial cytochrome P450s (CYPs) constitute an important family of monooxygenase enzymes that carry out essential roles in the metabolism of endogenous compounds and foreign chemicals. In the present work we report the characterization of CYP102A2 from B. subtilis with a focus on its substrate specificity. CYP102A2 is more active in oxidation of sodium dodecyl sulphate (SDS) than any other characterized CYP. The effect of SDS and NADPH concentration on reaction rate showed nonhyperbolic and hyperbolic dependence, respectively. The enzyme was found to exhibit a bell-shaped curve for plots of activity versus pH, over pH values 5.9-8.5. The rate of SDS oxidation reached the maximum value approximately at pH 7.2 and the pH transition observed controlled by two pK(a)s in the acidic (pK(a) = 6.7 ± 0.08) and basic (pK(a) = 7.3 ± 0.06) pH range. The results are discussed in relation to the future biotechnology applications of CYPs.
细菌细胞色素P450(CYPs)构成了一个重要的单加氧酶家族,在内源性化合物和外来化学物质的代谢中发挥着重要作用。在本研究中,我们报道了枯草芽孢杆菌CYP102A2的特性,重点关注其底物特异性。CYP102A2在氧化十二烷基硫酸钠(SDS)方面比任何其他已表征的CYP更具活性。SDS和NADPH浓度对反应速率的影响分别表现为非双曲线和双曲线依赖性。发现该酶在pH值5.9 - 8.5范围内,活性与pH的关系图呈现钟形曲线。SDS氧化速率在pH约7.2时达到最大值,观察到的pH转变由酸性(pK(a) = 6.7 ± 0.08)和碱性(pK(a) = 7.3 ± 0.06)pH范围内的两个pK(a)控制。结合CYPs未来的生物技术应用对结果进行了讨论。