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@article{1322953, author = {Shrivastava, Nidhi and Prokop, Zbyněk and Kumar, Ashwani}, article_location = {WASHINGTON, DC (USA)}, article_number = {21}, doi = {http://dx.doi.org/10.1128/AEM.01683-15}, keywords = {HALOALKANE DEHALOGENASE LINB; SPHINGOBIUM-INDICUM B90A; GAMMA-HEXACHLOROCYCLOHEXANE; BETA-HEXACHLOROCYCLOHEXANE; ALPHA-HEXACHLOROCYCLOHEXANE; DEGRADATION; TRANSFORMATION; ISOMERS}, language = {eng}, issn = {0099-2240}, journal = {Applied and Environmental Microbiology}, title = {Novel LinA Type 3 delta-Hexachlorocyclohexane Dehydrochlorinase}, url = {http://aem.asm.org/content/81/21/7553}, volume = {81}, year = {2015} }
TY - JOUR ID - 1322953 AU - Shrivastava, Nidhi - Prokop, Zbyněk - Kumar, Ashwani PY - 2015 TI - Novel LinA Type 3 delta-Hexachlorocyclohexane Dehydrochlorinase JF - Applied and Environmental Microbiology VL - 81 IS - 21 SP - 7553-7559 EP - 7553-7559 PB - AMER SOC MICROBIOLOGY SN - 00992240 KW - HALOALKANE DEHALOGENASE LINB KW - SPHINGOBIUM-INDICUM B90A KW - GAMMA-HEXACHLOROCYCLOHEXANE KW - BETA-HEXACHLOROCYCLOHEXANE KW - ALPHA-HEXACHLOROCYCLOHEXANE KW - DEGRADATION KW - TRANSFORMATION KW - ISOMERS UR - http://aem.asm.org/content/81/21/7553 L2 - http://aem.asm.org/content/81/21/7553 N2 - 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. ER -
SHRIVASTAVA, Nidhi, Zbyněk PROKOP and Ashwani KUMAR. Novel LinA Type 3 delta-Hexachlorocyclohexane Dehydrochlorinase. \textit{Applied and Environmental Microbiology}. WASHINGTON, DC (USA): AMER SOC MICROBIOLOGY, 2015, vol.~81, No~21, p.~7553-7559. ISSN~0099-2240. Available from: https://dx.doi.org/10.1128/AEM.01683-15.
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