Department of Life Sciences and Systems Biology, University of Torino, Via Accademia Albertina 13, 10123, Torino, Italy.
Department of Life Sciences and Systems Biology, University of Torino, Via Accademia Albertina 13, 10123, Torino, Italy.
Trends Biotechnol. 2021 Nov;39(11):1184-1207. doi: 10.1016/j.tibtech.2021.01.011. Epub 2021 Feb 18.
Members of class VII cytochromes P450 are catalytically self-sufficient enzymes containing a phthalate dioxygenase reductase-like domain fused to the P450 catalytic domain. Among these, CYP116B46 is the first enzyme for which the 3D structure of the whole polypeptide chain has been solved, shedding light on the interaction between its domains, which is crucial for catalysis. Most of these enzymes have been isolated from extremophiles or detoxifying bacteria that can carry out regio- and enantioselective oxidation of compounds of biotechnological interest. Protein engineering has generated mutants that can perform challenging organic reactions such as the anti-Markovnikov alkene oxidation. This potential, combined with the detailed 3D structure, forms the basis for further directed evolution studies aimed at widening their biotechnological exploitation.
VII 族细胞色素 P450 酶的成员是催化自足的酶,包含融合了 P450 催化结构域的邻苯二甲酸二氧酶还原酶样结构域。在这些酶中,CYP116B46 是第一个全多肽链 3D 结构被解决的酶,揭示了其结构域之间的相互作用,这对催化至关重要。这些酶大多数是从能够对具有生物技术意义的化合物进行区域和对映选择性氧化的极端微生物或解毒细菌中分离出来的。蛋白质工程已经产生了可以进行具有挑战性的有机反应的突变体,例如反马氏规则烯烃氧化。这种潜力,结合详细的 3D 结构,为进一步的定向进化研究奠定了基础,旨在扩大它们在生物技术中的应用。