Abstract

The study of the equilibrium of reactions catalyzed by thermostable enzymes is in demand for the development of biotechnological enzyme processes. The results of the analysis of equilibrium of transamination reaction catalyzed by thermostable transaminase from the archaeon Thermoproteus uzoniensis are presented below. A comparison of the conversion of substrates was performed for reactions with L-leucine and pyruvate and L-leucine and 2-oxobutyrate at 65°C. The establishment of the equilibrium was controlled by a decrease in the concentration of 2-oxobutyrate or pyruvate and by the accumulation of the keto analog of L-leucine. It was shown that the degree of conversion of L-leucine in the reaction with specific 2-oxobutyrate is higher than in the reaction with nonspecific pyruvate.

中文翻译：

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酮底物对乌兹多变形热菌转氨酶催化转氨反应产物收率的影响。

摘要

对热稳定酶催化的反应平衡的研究对于生物技术酶过程的发展是需要的。由古细菌Thermoproteus uzoniensis的热稳定转氨酶催化的转氨反应平衡分析结果如下。对于在65℃下与L-亮氨酸和丙酮酸以及L-亮氨酸和2-氧代丁酸的反应，进行了底物转化的比较。通过降低2-氧代丁酸或丙酮酸的浓度以及通过L-亮氨酸的酮类似物的积累来控制平衡的建立。结果表明，在与特定的2-氧代丁酸酯反应中，L-亮氨酸的转化程度高于与非特异性的丙酮酸的反应中。