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• W2024851405 startingPage "8244" @default.
• W2024851405 abstract "For the biocatalytic preparation of optically active amines, omega-transaminases (omega-TA) are of special interest since they allow the asymmetric synthesis starting from prostereogenic ketones with 100% yield. To facilitate the purification and characterization of novel omega-TA, a fast kinetic assay was developed based on the conversion of the widely used model substrate alpha-methylbenzylamine, which is commonly accepted by most of the known omega-TAs. The product from this reaction, acetophenone, can be detected spectrophotometrically at 245 nm with high sensitivity (epsilon = 12 mM(-1) cm(-1)), since the other reactants show only a low absorbance. Besides the standard substrate pyruvate, all low-absorbing ketones, aldehydes, or keto acids can be used as cosubstrates, and thus the amino acceptor specificity of a given omega-TA can be obtained quickly. Furthermore, the assay allows the fast investigation of enzymatic properties like pH and temperature optimum and stability. This method was used for the characterization of a novel omega-TA cloned from Rhodobacter sphaeroides, and the data obtained were in excellent accordance with a standard capillary electrophoresis assay." @default.
• W2024851405 created "2016-06-24" @default.
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• W2024851405 date "2009-09-09" @default.
• W2024851405 modified "2023-10-09" @default.
• W2024851405 title "Rapid and Sensitive Kinetic Assay for Characterization of ω-Transaminases" @default.
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• W2024851405 doi "https://doi.org/10.1021/ac901640q" @default.
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