Enzyme-substrate interaction and characterization of a 2,3-dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4.

Ang Li, Yuanyuan Qu, Jiti Zhou, Fang Ma

Journal: FEMS microbiology letters 2009;292(2):231-9

PMID: 19187202

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Abstract

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.

Address: Key Laboratory of Industrial Ecology and Environmental Engineering, School of Environmental and Biological Science and Technology, MOE, Dalian University of Technology, Dalian, China.

DOI: 10.1111/j.1574-6968.2009.01487.x

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MeSH Terms: Amino Acid Sequence, Bacterial Proteins, Cloning, Molecular, DNA, Bacterial, Dioxygenases, Escherichia coli, Kinetics, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Structure, Tertiary, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Substrate Specificity, Xanthomonadaceae