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Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites
R. Chaloupkova, T. Prudnikova, P. Rezacova, Z. Prokop, T. Koudelakova, L. Daniel, J. Brezovsky, W. Ikeda-Ohtsubo, Y. Sato, M. Kuty, Y. Nagata, I. Kuta Smatanova, J. Damborsky,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Principal Component Analysis MeSH
- Halogens metabolism MeSH
- Hydrolases chemistry metabolism MeSH
- Kinetics MeSH
- Crystallization MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
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- $a 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.
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