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

Release Time:2019-03-09  Hits:

Indexed by: Journal Article

Date of Publication: 2009-03-01

Journal: FEMS MICROBIOLOGY LETTERS

Included Journals: Scopus、PubMed、SCIE

Volume: 292

Issue: 2

Page Number: 231-239

ISSN: 0378-1097

Key Words: Dyella ginsengisoli; 2; 3-dihydroxybiphenyl 1; 2-dioxygenase; kinetic parameters; enzyme-substrate complex

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.

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