文献类型： 外文期刊

作者： Ren He-jun ¹ ; Lu Yang ² ; Zhou Rui ¹ ; Dai Chun-yan ³ ; Wang Yan ¹ ; Zhang Lan-ying ¹ ;

作者机构： 1.Jilin Univ, Coll Environm & Resources, Minist Educ, Key Lab Groudwater Resources & Environm, Changchun 130021, Peoples R China

2.Jilin Acad Agr Sci, Changchun 130033, Peoples R China

3.Jilin Univ, Hosp 1, Inst Virol & AIDS Res, Changchun 130061, Peoples R China

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+.