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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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