Department of Life Science and Biochemical Engineering, Sunmoon University, Asan 31460, Republic of Korea.
Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 02841, Republic of Korea.
J Microbiol Biotechnol. 2019 May 28;30(5):777-784. doi: 10.4014/jmb.1911.11048.
Self-sufficient P450s, due to their fused nature, are the most effective tools for electron transfer to activate C-H bonds. They catalyze the oxygenation of fatty acids at different omega positions. Here, two new, self-sufficient cytochrome P450s, named CYP102A15 and CYP102A170, from polar sp. PAMC 25034 and sp. PAMC 22724, respectively, were cloned and expressed in . The genes are homologues of CYP102A1 from . They catalyzed the hydroxylation of both saturated and unsaturated fatty acids ranging in length from C-C, with a moderately diverse profile compared to other members of the CYP102A subfamily. CYP102A15 exhibited the highest activity toward linoleic acid with K 15.3 μM, and CYP102A170 showed higher activity toward myristic acid with Km 17.4 μM. CYP10A170 also hydroxylated the Eicosapentaenoic acid at ω-1 position only. Various kinetic parameters of both monooxygenases were also determined.
由于其融合的性质，自给自足的 P450 是将电子转移到激活 C-H 键的最有效工具。它们催化脂肪酸在不同的ω位置的氧化。在这里，分别从极地 sp. PAMC 25034 和 sp. PAMC 22724 中克隆并表达了两种新的自给自足细胞色素 P450，命名为 CYP102A15 和 CYP102A170。这些基因是 CYP102A1 来自的同源物。它们催化 C-C 长度范围内的饱和和不饱和脂肪酸的羟化，与 CYP102A 亚家族的其他成员相比，具有中等多样化的特征。CYP102A15 对亚油酸的活性最高，K15.3 μM，CYP102A170 对肉豆蔻酸的 Km 17.4 μM 活性更高。CYP10A170 也只在 ω-1 位置羟基化二十碳五烯酸。还确定了这两种单加氧酶的各种动力学参数。
