Novel LinA Type 3 delta-Hexachlorocyclohexane Dehydrochlorinase

Investor logo

Warning

This publication doesn't include Faculty of Education. It includes Faculty of Science. Official publication website can be found on muni.cz.
Authors

SHRIVASTAVA Nidhi PROKOP Zbyněk KUMAR Ashwani

Year of publication 2015
Type Article in Periodical
Magazine / Source Applied and Environmental Microbiology
MU Faculty or unit

Faculty of Science

Citation
Web http://aem.asm.org/content/81/21/7553
Doi http://dx.doi.org/10.1128/AEM.01683-15
Field Biochemistry
Keywords HALOALKANE DEHALOGENASE LINB; SPHINGOBIUM-INDICUM B90A; GAMMA-HEXACHLOROCYCLOHEXANE; BETA-HEXACHLOROCYCLOHEXANE; ALPHA-HEXACHLOROCYCLOHEXANE; DEGRADATION; TRANSFORMATION; ISOMERS
Description LinA is the first enzyme of the microbial degradation pathway of a chlorinated insecticide, hexachlorocyclohexane (HCH), and mediates the dehydrochlorination of alpha-, gamma-, and delta-HCH. Its two variants, LinA type 1 and LinA type 2, which differ at 10 out of 156 amino acid residues, have been described. Their activities for the metabolism of different HCH isomers differ considerably but overall are high for gamma-HCH, moderate for alpha-HCH, low for delta-HCH, and lacking for beta-HCH. Here, we describe the characterization of a new variant of this enzyme, LinA type 3, whose gene was identified from the metagenome of an HCH-contaminated soil sample. Its deduced primary structure in the region spanning amino acid residues 1 to 147 of the protein exhibits 17 and 12 differences from LinA type 1 and LinA type 2, respectively. In addition, the residues GIHFAPS, present at the region spanning residues 148 to 154 in both LinA type 1 and LinA type 2, are deleted in LinA type 3. The activity of LinA type 3 for the metabolism of delta-HCH is several orders of magnitude higher than that of LinA type 1 or LinA type 2 and can be useful for improvement of the metabolism of delta-HCH.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.