ロード中...
Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine-200
Kinetic and spectroscopic studies have shown that the conserved active site residue His200 of the extradiol ring-cleaving homoprotocatechuate 2,3-dioxygenase (FeHPCD) from Brevibacterium fuscum is critical for efficient catalysis. The roles played by this residue are probed here by analysis of the s...
保存先:
| 出版年: | Biochemistry |
|---|---|
| 主要な著者: | , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2015
|
| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4558303/ https://ncbi.nlm.nih.gov/pubmed/26267790 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.5b00709 |
| タグ: |
タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!
|