Conformational changes allow processing of bulky substrates by a haloalkane dehalogenase with a small and buried active site.

ABSTRACT: Haloalkane dehalogenases catalyze the hydrolysis of halogen-carbon bonds in organic halogenated compounds and as such are of great utility as biocatalysts. The crystal structures of the haloalkane dehalogenase DhlA from the bacterium from Xanthobacter autotrophicus GJ10, specifically adapted for the conversion of the small 1,2-dichloroethane (DCE) molecule, display the smallest catalytic site (110 ų) within this enzyme family. However, during a substrate-specificity screening, we noted that DhlA can catalyze the conversion of far bulkier substrates, such as the 4-(bromomethyl)-6,7-dimethoxy-coumarin (220 ų). This large substrate cannot bind to DhlA without conformational alterations. These conformational changes have been previously inferred from kinetic anal

SUBMITTER: Kokkonen P 

PROVIDER: S-EPMC6065182 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature