| Title : Enzyme-substrate interaction and characterization of a 2,3-dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4 - Li_2009_FEMS.Microbiol.Lett_292_231 |
| Author(s) : Li A , Qu Y , Zhou J , Ma F |
| Ref : FEMS Microbiology Letters , 292 :231 , 2009 |
|
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. |
| PubMedSearch : Li_2009_FEMS.Microbiol.Lett_292_231 |
| PubMedID: 19187202 |
Li A, Qu Y, Zhou J, Ma F (2009)
Enzyme-substrate interaction and characterization of a 2,3-dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4
FEMS Microbiology Letters
292 :231
Li A, Qu Y, Zhou J, Ma F (2009)
FEMS Microbiology Letters
292 :231