Characterization of the Glutathione S-Transferases Involved in Styrene Degradation in Gordonia rubripertincta CWB2.

ABSTRACT: The glutathione S-transferases carried on the plasmid for the styrene-specific degradation pathway in the Actinobacterium Gordonia rubripertincta CWB2 were heterologously expressed in Escherichia coli. Both enzymes were purified via affinity chromatography and subjected to activity investigations. StyI and StyJ displayed activity toward the commonly used glutathione S-transferase model substrate 1-chloro-2,4-dinitrobenzene (CDNB) with K_m values of 0.0682 ± 0.0074 and 2.0281 ± 0.1301 mM and V_max values of 0.0158 ± 0.0002 and 0.348 ± 0.008 U mg^-1 for StyI and StyJ, respectively. The conversion of the natural substrate styrene oxide to the intermediate (1-phenyl-2-hydroxyethyl)glutathione was detected for StyI with 48.3 ± 2.9

SUBMITTER: Lienkamp AC 

PROVIDER: S-EPMC8552685 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature