7BX9

Purification, characterization and X-ray structure of YhdA-type azoreductase from Bacillus velezensis

7BX9 の概要

• エントリーDOI: 10.2210/pdb7bx9/pdb
• 分子名称: Azoreductase, GLYCEROL, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: azo reductase, azr, fmn, flavoprotein, oxidoreductase
• 由来する生物種: Bacillus amyloliquefaciens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19644.24

構造登録者

Khan, F.,Suguna, K. (登録日: 2020-04-18, 公開日: 2020-12-23, 最終更新日: 2023-11-29)

主引用文献

Bafana, A.,Khan, F.,Suguna, K.
Purification, characterization, and crystal structure of YhdA-type azoreductase from Bacillus velezensis.
Proteins, 89:483-492, 2021

PubMed Abstract: Azoreductases are being extensively investigated for their ability to initiate degradation of recalcitrant azo dyes through reduction of azo bonds. There is great interest in studying their diversity, structure, and function to facilitate better understanding and effective application. Current study reports azoreductase enzyme from Bacillus velezensis, which showed 69.5% identity to the Bacillus subtilis azoreductase YhdA. The enzyme was homotetrameric and molecular weight of each subunit was 20 kDa. It decolorized azo dyes with different structures. The V for decolorization of congo red, methyl orange and methyl red was 14.7, 28.6, and 77.9 nmol/min/mg, respectively. The enzyme contained FMN as cofactor and used NADPH as the favored co-substrate. It was oxygen-insensitive, but the presence of reducing agents enhanced its activity, which is a new finding. The azoreductase expression in B. velezensis was found to be unaffected by addition of azo dyes, although azo dyes are known to induce azoreductase expression in few organisms. The enzyme was thermostable with melting temperature of 89.5°C and functioned in wide temperature range. Further, the enzyme was crystallized and its structure was solved. The structural basis of its functional attributes is discussed. In our knowledge, this is the first report on characterization of azoreductase enzyme from B. velezensis.

PubMed: 33289153
DOI: 10.1002/prot.26032

実験手法

X-RAY DIFFRACTION (1.38 Å)