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- W1993747639 abstract "The crystal structure of the novel haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present in all structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift in the substrate-specificity class and were accompanied by a decrease in enzyme activity, stability and the elimination of substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step mediated by the lower basicity of the catalytic histidine." @default.
- W1993747639 created "2016-06-24" @default.
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- W1993747639 date "2014-06-29" @default.
- W1993747639 modified "2023-10-18" @default.
- W1993747639 title "Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites" @default.
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