Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

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CHALOUPKOVÁ Radka PRUDNIKOVA T. REZACOVA P. PROKOP Zbyněk KOUDELÁKOVÁ Táňa DANIEL Lukáš BREZOVSKÝ Jan IKEDA-OHTSUBO W. SATO Y. KUTY M. NAGATA Y. KUTA SMATANOVA I. DAMBORSKÝ Jiří

Rok publikování 2014
Druh Článek v odborném periodiku
Časopis / Zdroj Acta Crystallographica D
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Doi http://dx.doi.org/10.1107/S1399004714009018
Obor Biochemie
Klíčová slova haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94
Popis 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.
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