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Unusually Broad Substrate Profile of Self‐Sufficient Cytochrome P450 Monooxygenase CYP116B4 from Labrenzia aggregata
Author(s) -
Yin YueCai,
Yu HuiLei,
Luan ZhengJiao,
Li RenJie,
Ouyang PengFei,
Liu Jing,
Xu JianHe
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402309
Subject(s) - hydroxylation , cytochrome p450 , chemistry , monooxygenase , stereochemistry , catalysis , substrate (aquarium) , bicyclic molecule , biocatalysis , subfamily , molecule , organic chemistry , enzyme , biochemistry , biology , gene , ecology , ionic liquid
A new member of the CYP116B subfamily—P450 La MO —was discovered in Labrenzia aggregata by genomic data mining. It was successfully overexpressed in Escherichia coli , purified, and subsequently characterized spectroscopically, and its catalytic properties were assessed. Substrate profiling of the P450 La MO revealed that it was a versatile catalyst, exhibiting hydroxylation and epoxidation activities as well as O ‐dealkylation and asymmetric sulfoxidation activities. Diverse compounds, including alkylbenzenes, aromatic bicyclic molecules, and terpenoids, were shown to be hydroxylated by P450 La MO . Such diverse catalytic activities are uncommon for the bacterial P450s, and the P450 La MO ‐mediated stereoselective hydroxylation of inactivated CH bonds—ubiquitous and relatively unreactive in organic molecules—is particularly unusual. The self‐sufficient nature of P450 La MO , coupled with its broad substrate range, highlights it as an ideal template for directed evolution towards various applications.