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Title 

Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17

Authors 

Dockyu KimJ C ChaeJ Y JangG J ZylstraY M KimB S KangE Kim

Publisher 

Elsevier

Issue Date 

2005

Citation 

Biochemical and Biophysical Research Communications, vol. 326, no. 4, pp. 880-886

Keywords 

catechol 2,3-dioxygenasemolecular modelo-Xylenerhodococcuscatechol 2,3 dioxygenasecatechol derivativeguaiacolortho xylenetolueneamino acid sequence

Abstract 

Rhodococcus sp. strain DK17 is known to metabolize o-xylene and toluene through the intermediates 3,4-dimethylcatechol and 3- and 4-methylcatechol, respectively, which are further cleaved by a common catechol 2,3-dioxygenase. A putative gene encoding this enzyme (akbC) was amplified by PCR, cloned, and expressed in Escherichia coli. Assessment of the enzyme activity expressed in E. coli combined with sequence analysis of a mutant gene demonstrated that the akbC gene encodes the bona fide catechol 2,3-dioxygenase (AkbC) for metabolism of o-xylene and alkylbenzenes such as toluene and ethylbenzene. Analysis of the deduced amino acid sequence indicates that AkbC consists of a new catechol 2,3-dioxygenase class specific for methyl-substituted catechols. A computer-aided molecular modeling studies suggest that amino acid residues (particularly Phe177) in the β10-β11 loop play an essential role in characterizing the substrate specificity of AkbC.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2004.11.123

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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