酵母γ-谷氨酰激酶突变体的特性。
Characterization of γ-glutamyl kinase mutants from Saccharomyces cerevisiae.
机构信息
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
出版信息
J Biosci Bioeng. 2013 Nov;116(5):576-9. doi: 10.1016/j.jbiosc.2013.05.018. Epub 2013 Jun 14.
PMID:23770122
Abstract
We characterized the yeast γ-glutamyl kinase important for proline biosynthesis. Asp154 and Ile150 were involved in the affinity with glutamate as well as proline. The Asp154Asn and Ile150Thr mutants had increased thermostability, in addition to desensitization to proline. Deletion of a C-terminal domain dramatically decreased the reaction rate and stability.
摘要
我们对参与脯氨酸生物合成的酵母γ-谷氨酰激酶进行了研究。Asp154 和 Ile150 与谷氨酸和脯氨酸的亲和力有关。Asp154Asn 和 Ile150Thr 突变体的热稳定性增加，同时对脯氨酸的敏感性降低。C 端结构域的缺失显著降低了反应速率和稳定性。
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