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-Structure paper
| タイトル | Structural and catalytic insights into MhpB: A dioxygenase enzyme for degrading catecholic pollutants. |
|---|---|
| ジャーナル・号・ページ | J Hazard Mater, Vol. 488, Page 137431, Year 2025 |
| 掲載日 | 2025年1月28日 |
著者 | Xu Dong / Manli Xu / Miao Wu / Ying Wang / Xiaoqi Cheng / Wenxue Jiang / Dule Zheng / Ahmed Habiba Omar / Yibin Cheng / Aitao Li / Lixin Ma / Qiong Xing / ![]() |
| PubMed 要旨 | The increasing environmental pollution from persistent aromatic compounds requires effective biodegradation strategies. In this study, we focused on MhpB, an extradiol dioxygenase (EDO) from ...The increasing environmental pollution from persistent aromatic compounds requires effective biodegradation strategies. In this study, we focused on MhpB, an extradiol dioxygenase (EDO) from Escherichia coli. It is known for its role in the degradation of catechols, key intermediates in the degradation of aromatic compounds. We report the high-resolution structure of MhpB determined by cryo-electron microscopy, revealing a decameric conformation with the catalytic chamber at the side. The structure-based analysis allowed us to investigate the substrate-enzyme interaction and the substrate selectivity, which are crucial for its catalytic function. Site-directed mutagenesis was used to modulate the in vitro and in vivo substrate preference of MhpB, enhancing its potential for industrial applications in pollutant degradation. The study provides insight into the mechanism of the enzyme and paves the way for the development of engineered EDOs for environmental remediation of aromatic pollutants. |
リンク | J Hazard Mater / PubMed:39892151 |
| 手法 | EM (単粒子) |
| 解像度 | 2.59 - 2.72 Å |
| 構造データ | EMDB-36757, PDB-8k04: EMDB-62561, PDB-9kti: |
| 化合物 | ![]() ChemComp-FE2: ![]() PDB-1eg2: |
| 由来 |
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キーワード | BIOSYNTHETIC PROTEIN / dioxygenase / 2 / 3-hydroxycinnamic acid 1 / 2-dioxygenase |
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