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Substrate Selectivity and Biochemical Properties of 4-Hydroxy-2-Keto-Pentanoic Acid Aldolase from Escherichia coli

机译:大肠杆菌4-羟基-2-酮-戊酸醛缩酶的底物选择性和生化特性

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摘要

4-Hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli was identified as a class I aldolase. The enzyme was found to be highly selective for the acetaldehyde acceptor but would accept α-ketobutyric acid or phenylpyruvic acid in place of the pyruvic acid carbonyl donor.
机译:来自大肠杆菌的4-羟基-2-酮-戊酸醛缩酶被鉴定为I类醛缩酶。发现该酶对乙醛受体具有高度选择性,但可以接受α-酮丁酸或苯丙酮酸代替丙酮酸羰基供体。

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