Detailed Information on Publication Record
2015
Novel LinA Type 3 delta-Hexachlorocyclohexane Dehydrochlorinase
SHRIVASTAVA, Nidhi, Zbyněk PROKOP and Ashwani KUMARBasic information
Original name
Novel LinA Type 3 delta-Hexachlorocyclohexane Dehydrochlorinase
Authors
SHRIVASTAVA, Nidhi (356 India), Zbyněk PROKOP (203 Czech Republic, belonging to the institution) and Ashwani KUMAR (356 India, guarantor)
Edition
Applied and Environmental Microbiology, WASHINGTON, DC (USA), AMER SOC MICROBIOLOGY, 2015, 0099-2240
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 3.823
RIV identification code
RIV/00216224:14310/15:00085588
Organization unit
Faculty of Science
UT WoS
000363462900021
Keywords in English
HALOALKANE DEHALOGENASE LINB; SPHINGOBIUM-INDICUM B90A; GAMMA-HEXACHLOROCYCLOHEXANE; BETA-HEXACHLOROCYCLOHEXANE; ALPHA-HEXACHLOROCYCLOHEXANE; DEGRADATION; TRANSFORMATION; ISOMERS
Tags
International impact, Reviewed
Změněno: 17/3/2016 14:09, Mgr. Michaela Hylsová, Ph.D.
Abstract
V originále
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.
Links
LM2011028, research and development project |
| ||
LO1214, research and development project |
|