两种自给自足单加氧酶 CYP102A15 和 CYP102A170 的特性鉴定为长链脂肪酸羟化酶。
Characterization of Two Self-Sufficient Monooxygenases, CYP102A15 and CYP102A170, as Long-Chain Fatty Acid Hydroxylases.
机构信息
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.
出版信息
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。
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