8WWU の概要
| エントリーDOI | 10.2210/pdb8wwu/pdb |
| 分子名称 | Glutamine synthetase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MANGANESE (II) ION, ... (5 entities in total) |
| 機能のキーワード | glutamine synthetase, 1-naphthylamine glutamine synthetase, ligase |
| 由来する生物種 | Pseudomonas lactis |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 345442.67 |
| 構造登録者 | |
| 主引用文献 | Zhang, S.T.,Deng, S.K.,Li, T.,Maloney, M.E.,Li, D.F.,Spain, J.C.,Zhou, N.Y. Discovery of the 1-naphthylamine biodegradation pathway reveals a broad-substrate-spectrum enzyme catalyzing 1-naphthylamine glutamylation. Elife, 13:-, 2024 Cited by PubMed Abstract: 1-Naphthylamine (1NA), which is harmful to human and aquatic animals, has been used widely in the manufacturing of dyes, pesticides, and rubber antioxidants. Nevertheless, little is known about its environmental behavior and no bacteria have been reported to use it as the growth substrate. Herein, we describe a pathway for 1NA degradation in the isolate sp. strain JS3066, determine the structure and mechanism of the enzyme NpaA1 that catalyzes the initial reaction, and reveal how the pathway evolved. From genetic and enzymatic analysis, a five gene-cluster encoding a dioxygenase system was determined to be responsible for the initial steps in 1NA degradation through glutamylation of 1NA. The γ-glutamylated 1NA was subsequently oxidized to 1,2-dihydroxynaphthalene which was further degraded by the well-established pathway of naphthalene degradation via catechol. A glutamine synthetase-like (GS-like) enzyme (NpaA1) initiates 1NA glutamylation, and this enzyme exhibits a broad substrate selectivity toward a variety of anilines and naphthylamine derivatives. Structural analysis revealed that the aromatic residues in the 1NA entry tunnel and the V201 site in the large substrate-binding pocket significantly influence NpaA1's substrate preferences. The findings enhance understanding of degrading polycyclic aromatic amines, and will also enable the application of bioremediation at naphthylamine contaminated sites. PubMed: 39163210DOI: 10.7554/eLife.95555 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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