. . "47818" . . "Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites." . "Prokop, Zbyn\u011Bk" . "000338917000009" . "haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94"@en . "RIV/00216224:14310/14:00074206!RIV15-MSM-14310___" . "[42A70CDB78D1]" . "Daniel, Luk\u00E1\u0161" . "RIV/00216224:14310/14:00074206" . . "Chaloupkov\u00E1, Radka" . . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . "Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites."@en . "I, P(GAP207/12/0775), P(LO1214), S" . "14310" . . "Brezovsk\u00FD, Jan" . "Crystal structure of novel haloalkane dehalogenase DbeA 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 of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step, mediated by lower basicity of the catalytic histidine."@en . "Nagata, Y." . . . "70" . . . . . "July" . "Kuta Smatanova, I." . "Rezacova, P." . "Ikeda-Ohtsubo, W." . "Koudel\u00E1kov\u00E1, T\u00E1\u0148a" . . "Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites." . "Kuty, M." . . . . "10.1107/S1399004714009018" . . "14"^^ . . . "0907-4449" . "Prudnikova, T." . "Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites."@en . "Sato, Y." . "13"^^ . . "Damborsk\u00FD, Ji\u0159\u00ED" . "Acta Crystallographica D" . . "6"^^ . "Crystal structure of novel haloalkane dehalogenase DbeA 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 of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step, mediated by lower basicity of the catalytic histidine." .