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

doi:10.1111/j.1574-6968.2009.01487.x

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

^*Corresponding author for this work

School of Environment

Dalian University of Technology

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

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.

Original language	English
Pages (from-to)	231-239
Number of pages	9
Journal	FEMS Microbiology Letters
Volume	292
Issue number	2
DOIs	https://doi.org/10.1111/j.1574-6968.2009.01487.x
State	Published - Mar 2009

Keywords

2,3-dihydroxybiphenyl 1,2-dioxygenase
Dyella ginsengisoli
Enzyme-substrate complex
Kinetic parameters

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10.1111/j.1574-6968.2009.01487.x

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

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 (Kcat/Km) 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.",

keywords = "2,3-dihydroxybiphenyl 1,2-dioxygenase, Dyella ginsengisoli, Enzyme-substrate complex, Kinetic parameters",

author = "Ang Li and Yuanyuan Qu and Jiti Zhou and Fang Ma",

year = "2009",

month = mar,

doi = "10.1111/j.1574-6968.2009.01487.x",

language = "英语",

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T1 - Enzyme-substrate interaction and characterization of a 2,3- dihydroxybiphenyl 1,2-dioxygenase from Dyella ginsengisoli LA-4

AU - Li, Ang

AU - Qu, Yuanyuan

AU - Zhou, Jiti

AU - Ma, Fang

PY - 2009/3

Y1 - 2009/3

N2 - 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 (Kcat/Km) 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.

AB - 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 (Kcat/Km) 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.

KW - 2,3-dihydroxybiphenyl 1,2-dioxygenase

KW - Dyella ginsengisoli

KW - Enzyme-substrate complex

KW - Kinetic parameters

UR - https://www.scopus.com/pages/publications/60349085042

U2 - 10.1111/j.1574-6968.2009.01487.x

DO - 10.1111/j.1574-6968.2009.01487.x

M3 - 文章

C2 - 19187202

AN - SCOPUS:60349085042

SN - 0378-1097

VL - 292

SP - 231

EP - 239

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

IS - 2

ER -

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

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Keywords

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