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

Varování

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

Autoři	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.
Související projekty:	Centrum pro výzkum toxických látek v prostředí Structure-functional Relationships of Haloalkane Dehalogenases Centrum pro výzkum toxických látek v prostředí