| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 20555 | Journal of Bioscience and Bioengineering | 2013 | 4 Pages |
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.
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Physical Sciences and Engineering
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Authors
Yuki Tatehashi, Hiroshi Takagi,