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• W2045490589 abstract "Background Here 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 Findings Enzyme kinetic studies were performed with purified LinA variants. Models of LinA2B90A A110T, A111C, A110T/A111C and LinA1B90A 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." @default.
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• W2045490589 date "2011-09-16" @default.
• W2045490589 modified "2023-10-05" @default.
• W2045490589 title "Kinetic and Sequence-Structure-Function Analysis of Known LinA Variants with Different Hexachlorocyclohexane Isomers" @default.
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• W2045490589 doi "https://doi.org/10.1371/journal.pone.0025128" @default.
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