Evidence map›Paper›PMID 21949868›Full record

ArticlePloS one2011

Kinetic and sequence-structure-function analysis of known LinA variants with different hexachlorocyclohexane isomers.

Pooja Sharma, Rinku Pandey, Kirti Kumari, Gunjan Pandey, Colin J Jackson, Robyn J Russell, John G Oakeshott, Rup Lal

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Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Pooja SharmaDepartment of Zoology, University of Delhi, Delhi, India.
Rinku Pandey
Kirti Kumari
Gunjan Pandey
Colin J Jackson
Robyn J Russell
John G Oakeshott
Rup Lal

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHere we report specific activities of all seven naturally occurring LinA variants towards three different isomers, α, γ and δ, of a priority persistent pollutant, hexachlorocyclohexane (HCH). Sequence-structure-function differences contributing to the differences in their stereospecificity for α-, γ-, and δ-HCH and enantiospecificity for (+)- and (-)-α -HCH are also discussed. METHODOLOGY/PRINCIPAL

findingsEnzyme kinetic studies were performed with purified LinA variants. Models of LinA2(B90A) A110T, A111C, A110T/A111C and LinA1(B90A) were constructed using the FoldX computer algorithm. Turnover rates (min(-1)) showed that the LinAs exhibited differential substrate affinity amongst the four HCH isomers tested. α-HCH was found to be the most preferred substrate by all LinA's, followed by the γ and then δ isomer. CONCLUSIONS/SIGNIFICANCE: The kinetic observations suggest that LinA-γ1-7 is the best variant for developing an enzyme-based bioremediation technology for HCH. The majority of the sequence variation in the various linA genes that have been isolated is not neutral, but alters the enantio- and stereoselectivity of the encoded proteins.

Indexed as

AnticonvulsantsBacterial ProteinsBiodegradation, EnvironmentalEscherichia coliGenetic VariationHexachlorocyclohexaneKineticsLyasesModels, ChemicalStereoisomerismAnticonvulsantsBacterial ProteinsHexachlorocyclohexaneLyases

Identifiers

PMID21949868
PMCPMC3174995

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.