Crystallization and preliminary characterization of chloromuconolactone dehalogenase from Rhodococcus opacus 1CP.

ABSTRACT: Chloroaromatic compounds are often very persistent environmental pollutants. Nevertheless, numerous bacteria are able to metabolize these compounds and to utilize them as sole energy and carbon sources. Rhodococcus opacus 1CP is able to degrade several chloroaromatic compounds, some of them via a variation of the 3-chlorocatechol branch of the modified ortho-cleavage pathway. This branch in R. opacus differs from that in Proteobacteria in the inability of the chloromuconate cycloisomerase to dehalogenate. Instead, a unique enzyme designated as chloromuconolactone dehalogenase (ClcF) is recruited. ClcF dehalogenates 5-chloromuconolactone to cis-dienelactone and shows a high similarity to muconolactone isomerases (EC 5.3.3.4). However, unlike the latter enzymes, it is unable to catalyse the

SUBMITTER: Roth C 

PROVIDER: S-EPMC3374520 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature