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首页> 外文期刊>Applied Microbiology >Distinct Regioselectivity of Fungal P450 Enzymes for Steroidal Hydroxylation
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Distinct Regioselectivity of Fungal P450 Enzymes for Steroidal Hydroxylation

机译：真菌P450酶对甾体羟基化的不同区域选择性

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In this study, we identified two P450 enzymes (CYP5150AP3 and CYP5150AN1) from Thanatephorus cucumeris NBRC 6298 by combination of transcriptome sequencing and heterologous expression in Pichia pastoris. The biotransformation of 11-deoxycortisol and testosterone by Pichia pastoris whole cells coexpressing the cyp5150ap3 and por genes demonstrated that the CYP5150AP3 enzyme possessed steroidal 7β-hydroxylase activities toward these substrates, and the regioselectivity was dependent on the structures of steroidal compounds. CYP5150AN1 catalyzed the 2β-hydroxylation of 11-deoxycortisol. It is interesting that they display different regioselectivity of hydroxylation from that of their isoenzyme, CYP5150AP2, which possesses 19- and 11β-hydroxylase activities.IMPORTANCE The steroidal hydroxylases CYP5150AP3 and CYP5150AN1 together with the previously characterized CYP5150AP2 belong to the CYP5150A family of P450 enzymes with high amino acid sequence identity, but they showed completely different regioselectivities toward 11-deoxycortisol, suggesting the regioselectivity diversity of steroidal hydroxylases of CYP5150 family. They are also distinct from the known bacterial and fungal steroidal hydroxylases in substrate specificity and regioselectivity. Biocatalytic hydroxylation is one of the important transformations for the functionalization of steroid nucleus rings but remains a very challenging task in organic synthesis. These hydroxylases are useful additions to the toolbox of hydroxylase enzymes for the functionalization of steroids at various positions.
机译：在这项研究中，我们通过转录组测序和异源表达在巴斯德毕赤酵母中鉴定了来自丘脑Thanatephorus cucumeris NBRC 6298的两种P450酶（CYP5150AP3和CYP5150AN1）。共表达cyp5150ap3和por基因的巴斯德毕赤酵母全细胞对11-脱氧皮质醇和睾丸酮的生物转化表明，CYP5150AP3酶对这些底物具有甾体7β-羟化酶活性，区域选择性取决于甾体化合物的结构。 CYP5150AN1催化11-脱氧皮质醇的2β-羟基化。有趣的是，它们与具有19-和11β-羟化酶活性的同工酶CYP5150AP2表现出不同的羟化区域选择性。高氨基酸序列同一性，但它们对11-脱氧皮质醇显示完全不同的区域选择性，这表明CYP5150家族的甾体羟化酶的区域选择性多样性。它们在底物特异性和区域选择性方面也不同于已知的细菌和真菌甾族羟化酶。生物催化羟基化是类固醇核环功能化的重要转变之一，但在有机合成中仍然是一项非常艰巨的任务。这些羟化酶是羟化酶工具箱中有用的添加物，用于甾体在各个位置的功能化。

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