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个人信息Personal Information
教授
博士生导师
硕士生导师
性别:男
毕业院校:大连工学院
学位:硕士
所在单位:环境学院
电子邮箱:zjiti@dlut.edu.cn
Enzyme-substrate interaction and characterization of a 2,3-dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4
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论文类型:期刊论文
发表时间:2009-03-01
发表刊物:FEMS MICROBIOLOGY LETTERS
收录刊物:SCIE、PubMed、Scopus
卷号:292
期号:2
页面范围:231-239
ISSN号:0378-1097
关键字:Dyella ginsengisoli; 2; 3-dihydroxybiphenyl 1; 2-dioxygenase; kinetic parameters; enzyme-substrate complex
摘要:A bphC gene (915 bp) encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) was amplified by PCR from Dyella ginsengisoli LA-4, which was heterologously expressed in Escherichia coli. The purified His-Tag BphC was able to catalyze the meta-cleavage reaction of the dihydroxylated aromatic rings. According to the specificity constant (K-cat/K-m) of BphC_LA-4, the specificity of BphC_LA-4 was determined in the following order: 2,3-dihydroxybiphenyl > 3-methylcatechol > catechol > 4-chlorocatechol > 4-methylcatechol. The experimental data were consistent with the prediction of enzyme-substrate complexes. The highest specific activity of BphC_LA-4 was 118.3 U mg(-1) for 2,3-dihydroxybiphenyl.