論文 - 詳細
| RRC ID | 54945 |
|---|---|
| 著者 | Okamura E, Hirai MY. |
| タイトル | Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana. |
| ジャーナル | Sci Rep |
| Abstract |
The proteinogenic amino acid L-serine is a precursor for various essential biomolecules in all organisms. 3-Phosphoglycerate dehydrogenase (PGDH) is the first committed enzyme of the phosphorylated pathway of L-serine biosynthesis, and is regulated by negative feedback from L-serine in bacteria and plants. In the present study, two Arabidopsis PGDH isoforms were inhibited by L-serine but were activated by L-amino acids such as L-homocysteine in vitro. Activation and inhibition by these amino acids was cooperative, suggesting an allosteric mechanism. Moreover, the half maximal effective concentration of L-homocysteine was 2 orders of magnitude lower than that of L-serine, suggesting greater regulatory potency. These are the first data to show that PGDH is activated by various biomolecules and indicate that serine biosynthesis is regulated by multiple pathways. |
| 巻・号 | 7(1) |
| ページ | 3533 |
| 公開日 | 2017-6-14 |
| DOI | 10.1038/s41598-017-03807-5 |
| PII | 10.1038/s41598-017-03807-5 |
| PMID | 28615699 |
| PMC | PMC5471267 |
| MeSH | Allosteric Regulation Arabidopsis / enzymology* Arabidopsis / metabolism* Arabidopsis Proteins / metabolism* Enzyme Activators / metabolism Enzyme Inhibitors / metabolism Gene Expression Regulation, Enzymologic* Gene Expression Regulation, Plant* Phosphoglycerate Dehydrogenase / metabolism* Serine / biosynthesis* |
| IF | 4.011 |
| 引用数 | 10 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Blogs |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| シロイヌナズナ / 植物培養細胞・遺伝子 | pda02295 pda04481 |