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• W2610736062 startingPage "1482" @default.
• W2610736062 abstract "Amine transaminase (ATA) catalyse enantioselectively the direct amination of ketones, but insufficient stability during catalysis limits their industrial applicability. Recently, we revealed that ATAs suffer from substrate-induced inactivation mechanism involving dissociation of the enzyme-cofactor intermediate. Here, we report on engineering the cofactor-ring-binding element, which also shapes the active-site entrance. Only two point mutations in this motif improved temperature and catalytic stability in both biphasic media and organic solvent. Thermodynamic analysis revealed a higher melting point for the enzyme-cofactor intermediate. The high cofactor affinity eliminates the need for pyridoxal 5'-phosphate supply, thus making large-scale reactions more cost effective. This is the first report on stabilising a tetrameric ATA by mutating a single structural element. As this structural hotspot is a common feature of other transaminases it could serve as a general engineering target." @default.
• W2610736062 created "2017-05-12" @default.
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• W2610736062 date "2017-06-13" @default.
• W2610736062 modified "2023-09-24" @default.
• W2610736062 title "Three in One: Temperature, Solvent and Catalytic Stability by Engineering the Cofactor-Binding Element of Amine Transaminase" @default.
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• W2610736062 doi "https://doi.org/10.1002/cbic.201700236" @default.
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