Molecular Cloning and Characterization of a New Cold-active Extradiol Dioxygenase from a Metagenomic Library Derived from Polychlorinated Biphenyl-contaminated Soil

文献类型： 外文期刊

第一作者： Ren He-jun

作者： Ren He-jun;Zhou Rui;Wang Yan;Zhang Lan-ying;Lu Yang;Dai Chun-yan

作者机构：

关键词： Extradiol dioxygenase;Metagenome;Cold-active enzyme;Gene cloning;Functional characterization

期刊名称：CHEMICAL RESEARCH IN CHINESE UNIVERSITIES （ 影响因子：1.307； 五年影响因子：0.979 ）

ISSN： 1005-9040

年卷期： 2012 年 28 卷 4 期

页码：

收录情况： SCI

摘要： To find new extradiol dioxygenases(EDOs, EC 1.13.11.2), a metagenomics library was constructed from polychlorinated biphenyl-contaminated soil and was screened for some dioxygenase with aromatic ring cleavage activity. A novel EDO, designated as BphC_A, was identified and heterologously expressed in Escherichia coli. The deduced amino acid sequence of BphC_A exhibited a homology of less than 60% with other known EDOs. Phylogenetic analysis of BphC_A suggests that the protein is a novel member of the EDO family. The enzyme exhibits higher substrate affinity and catalytic efficiency toward 3-methylcatechol than toward 2,3-dihydroxybiphenyl or catechol, the preferred substrate of other known EDOs. The optimum activity of purified BphC_A occurred at pH=8.5 and 35 degrees C, and BphC_A showed more than 40% of its initial activity at 5 degrees C. The activity of purified BphC_A was significantly induced by Mn2+ and slightly reduced by Al3+, Cu2+ and Zn2+.

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