Characterisation of CYP102A25 from Bacillus marmarensis and CYP102A26 from Pontibacillus halophilus: P450 Homologues of BM3 with Preference towards Hydroxylation of Medium‐Chain Fatty Acids,ChemBioChem

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Characterisation of CYP102A25 from Bacillus marmarensis and CYP102A26 from Pontibacillus halophilus: P450 Homologues of BM3 with Preference towards Hydroxylation of Medium‐Chain Fatty Acids
ChemBioChem ( IF 2.6 ) Pub Date : 2018-02-05 , DOI: 10.1002/cbic.201700598
Joanne L Porter ₁ , Jack Manning ₁ , Selina Sabatini ₁ , Michele Tavanti ₁ , Nicholas J Turner ₁ , Sabine L Flitsch ₁

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A new twist: Here new alternatives to the well‐studied prototype self‐sufficient CYP102A1 (P450 BM3) are presented. The new BM3 homologues, CYP102A25 (BMar) and CYP102A26 (PHal), have different substrate profiles encompassing saturated and unsaturated fatty acids. PHal also displays higher regioselectivity for the production of the ω−2 hydroxy acid than previously reported.

中文翻译：

Bacillus marmarensis 的 CYP102A25 和 Pontibacillus halophilus 的 CYP102A26 的表征：BM3 的 P450 同系物，偏向于中链脂肪酸的羟基化

一个新的转折：这里介绍了经过充分研究的原型自给自足 CYP102A1 (P450 BM3) 的新替代品。新的 BM3 同系物 CYP102A25 (BMar) 和 CYP102A26 (PHal) 具有不同的底物谱，包括饱和和不饱和脂肪酸。PHal 对 ω-2 羟基酸的生产也表现出比以前报道的更高的区域选择性。

更新日期：2018-02-05

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