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

• Autoři: 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
• www: Full Text
• Doi: https://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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