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首页> 外文期刊>Catalysis science & technology >Structure of the fungal hydroxylase, CYP505A30, and rational transfer of mutation data from CYP102A1 to alter regioselectivity
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Structure of the fungal hydroxylase, CYP505A30, and rational transfer of mutation data from CYP102A1 to alter regioselectivity

机译：CYP505A30真菌羟化酶的结构,和理性的突变的数据转移CYP102A1改变区域选择性

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摘要

CYP505A30 is a fungal, self-sufficient cytochrome P450 monooxygenase that can selectively oxyfunctionalise n-alkanes, fatty alcohols, and fatty acids. From alkanes, it produces a mixture of non-vicinal diols by two sequential hydroxylation reactions. Here we report the structure of the haem domain of CYP505A30, the first structure for a member of the CYP505 family, with dodecanoic acid bound within the active site. Overall, a high structural similarity to the related bacterial CYP102A1 was observed, despite low sequence identity (<40%). Comparison of the active sites, however, showed a high degree of conservation with only two amino acid differences close to the haem. Stabilisation of the fatty acid substrate in CYP505A30 also occurs, as in CYP102A1, via an arginine residue. However, compared to R47, which is situated in the beta 1 region of CYP102A1, R358 is located in the beta 3 region of CYP505A30. We furthermore created mutants to test if it is possible to rationally transfer the knowledge on active site mutations in CYP102A1 to change the regioselectivity of CYP505A30. The introduction of F93V, I334F mutations resulted in increased omega-1 (C2) regioselectivity, similar to CYP102A1 87-328, of more than 80% for n-octane and 90% for n-decane. Changing residues to resemble the CYP102A1 wildtype increased the regioselectivity towards omega-2 (C3) to over 60% for both substrates. The knowledge gained from this study unlocks a more selective production of symmetrical non-vicinal diols from n-alkanes.
机译：CYP505A30是一种真菌,自给自足的细胞色素可以有选择地P450单氧酶oxyfunctionalise正烷烃、脂肪醇和脂肪酸。由两个连续的non-vicinal二醇羟基化反应。CYP505A30的血红素结构域首先对CYP505成员结构家庭,月桂酸中活跃的站点。相似的相关细菌CYP102A1观察到,尽管低序列标识(< 40%)。比较活跃的网站,然而,显示高度的保护只有两个氨基酸酸的差异接近血红素。CYP505A30脂肪酸底物的发生,在CYP102A1,通过精氨酸残基。然而,位于R47相比CYP102A1 beta 1地区,R358位于β3 CYP505A30地区。如果是可能创造突变体测试理性知识转移活性部位突变CYP102A1改变CYP505A30的区域选择性。F93V, I334F突变导致增加ω₁(C2)区域选择性,类似CYP102A1 87 - 328年,超过80%的n-octane, n-decane为90%。类似于CYP102A1野生型增加了区域选择性对omega-2 (C3)超过60%基板。本研究打开一个更有选择性的生产对称non-vicinal从链烷二醇。

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