5K8M

Apo 5-nitroanthranilate aminohydrolase

5K8M の概要

• エントリーDOI: 10.2210/pdb5k8m/pdb
• 関連するPDBエントリー: 5K8N 5K8O 5K8P
• 分子名称: 5-nitroanthranilic acid aminohydrolase (1 entity in total)
• 機能のキーワード: nitroaromatics, deaminase, metalloenzyme, hydrolase
• 由来する生物種: Bradyrhizobium sp.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 187853.17

構造登録者

Kalyoncu, S. (登録日: 2016-05-30, 公開日: 2016-10-05, 最終更新日: 2024-11-13)

主引用文献

Kalyoncu, S.,Heaner, D.P.,Kurt, Z.,Bethel, C.M.,Ukachukwu, C.U.,Chakravarthy, S.,Spain, J.C.,Lieberman, R.L.
Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.
Nat.Chem.Biol., 12:1031-1036, 2016

PubMed Abstract: Nitroaromatic compounds are typically toxic and resistant to degradation. Bradyrhizobium species strain JS329 metabolizes 5-nitroanthranilic acid (5NAA), which is a molecule secreted by Streptomyces scabies, the plant pathogen responsible for potato scab. The first biodegradation enzyme is 5NAA-aminohydrolase (5NAA-A), a metalloprotease family member that converts 5NAA to 5-nitrosalicylic acid. We characterized 5NAA-A biochemically and obtained snapshots of its mechanism. 5NAA-A, an octamer that can use several divalent transition metals for catalysis in vitro, employs a nucleophilic aromatic substitution mechanism. Unexpectedly, the metal in 5NAA-A is labile but is readily loaded in the presence of substrate. 5NAA-A is specific for 5NAA and cannot hydrolyze other tested derivatives, which are likewise poor inhibitors. The 5NAA-A structure and mechanism expand our understanding of the chemical ecology of an agriculturally important plant and pathogen, and will inform bioremediation and biocatalytic approaches to mitigate the environmental and ecological impact of nitroanilines and other challenging substrates.

PubMed: 27694799
DOI: 10.1038/nchembio.2191

実験手法

X-RAY DIFFRACTION (2.75 Å)