Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane.

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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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MORIUCHI Ryota TANAKA Hiroki NIKAWADORI Yuki ISHITSUKA Mayuko ITO Michihiro OHTSUBO Yoshiyuki TSUDA Masataka DAMBORSKÝ Jiří PROKOP Zbyněk NAGATA Yuji

Rok publikování 2014
Druh Článek v odborném periodiku
Časopis / Zdroj Applied Microbiology and Biotechnology Express
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
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Doi http://dx.doi.org/10.1186/s13568-014-0072-5
Obor Biochemie
Klíčová slova beta -Hexachlorocyclohexane; Xenobiotics; Biodegradation; Haloalkane dehalogenase; Protein evolution
Popis Two haloalkane dehalogenases, LinBUT and LinBMI, each with 296 amino acid (aa) residues, exhibit only seven amino acid residue differences between them, but LinBMI‘s catalytic performance towards beta-hexachlorocyclohexane (beta-HCH) is considerably higher than LinBUT‘s. To elucidate the molecular basis governing this difference, intermediate mutants between LinBUT and LinBMI were constructed and kinetically characterized. The activities of LinBUT-based mutants gradually increased by cumulative mutations into LinBUT, and the effects of the individual amino acid substitutions depended on combination with other mutations. These results indicated that LinBUT‘s b-HCH degradation activity can be enhanced in a stepwise manner by the accumulation of point mutations.
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