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

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 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

SUBMITTER: Sharma P 

PROVIDER: S-EPMC3174995 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature