6QZO

Crystal structure of DyP-type peroxidase from Cellulomonas bogoriensis

6QZO の概要

• エントリーDOI: 10.2210/pdb6qzo/pdb
• 分子名称: Peroxidase, PROTOPORPHYRIN IX CONTAINING FE, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Cellulomonas bogoriensis 69B4 = DSM 16987
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 336733.79

構造登録者

Rozeboom, H.J.,Fraaije, M.W. (登録日: 2019-03-12, 公開日: 2019-04-03, 最終更新日: 2024-01-24)

主引用文献

Habib, M.H.,Rozeboom, H.J.,Fraaije, M.W.
Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis.
Molecules, 24:-, 2019

PubMed Abstract: DyP-type peroxidases are heme-containing enzymes that have received increasing attention over recent years with regards to their potential as biocatalysts. A novel DyP-type peroxidase (DyP) was discovered from the alkaliphilic cellulomonad, , which could be overexpressed in . The biochemical characterization of the recombinant enzyme showed that it is a heme-containing enzyme capable to act as a peroxidase on several dyes. With the tested substrates, the enzyme is most active at acidic pH values and is quite tolerant towards solvents. The crystal structure of DyP was solved which revealed atomic details of the dimeric heme-containing enzyme. A peculiar feature of DyP is the presence of a glutamate in the active site which in most other DyPs is an aspartate, being part of the DyP-typifying sequence motif GXXDG. The E201D DyP mutant was prepared and analyzed which revealed that the mutant enzyme shows a significantly higher activity on several dyes when compared with the wild-type enzyme.

PubMed: 30934796
DOI: 10.3390/molecules24071208

実験手法

X-RAY DIFFRACTION (2.4 Å)