8S6C

Crystal structure of Cyanobacterium TDX16 peroxidase

8S6C の概要

• エントリーDOI: 10.2210/pdb8s6c/pdb
• 分子名称: Lactoperoxidase, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: heme, oxidoreductase
• 由来する生物種: cyanobacterium TDX16
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57638.13

構造登録者

Rozeboom, H.J.,Savino, S.,Fraaije, M.W. (登録日: 2024-02-27, 公開日: 2024-12-04, 最終更新日: 2025-02-05)

主引用文献

Pecanac, O.,Martin, C.,Savino, S.,Rozeboom, H.J.,Fraaije, M.W.,Loncar, N.
Biochemical and Structural Characterisation of a Bacterial Lactoperoxidase.
Chembiochem, 26:e202400713-e202400713, 2025

PubMed Abstract: Peroxidases belong to a group of enzymes that are widely found in animals, plants and microorganisms. These enzymes are effective biocatalysts for a wide range of oxidations on various substrates. This work presents a biochemical and structural characterization of a novel heme-containing peroxidase from Cyanobacterium sp. TDX16, CyanoPOX. This cyanobacterial enzyme was successfully overexpressed in Escherichia coli as a soluble, heme-containing monomeric enzyme. Although CyanoPOX shares relatively low sequence identity (37%) with bovine lactoperoxidase, it displays comparable biochemical properties. CyanoPOX is most stable and active in slightly acidic conditions (pH 6-6.5) and moderately thermostable (melting temperature around 48 °C). Several compounds that are typical substrates for mammalian lactoperoxidases were tested to establish the catalytic potential of CyanoPOX. Potassium iodide showed the highest catalytic efficiency (126 mM-1s-1), while various aromatic compounds were also readily converted. Structural elucidation of CyanoPOX confirmed the presence of a non-covalently bound b-type heme cofactor that is situated in the central core of the protein. Except for a highly similar overall structure, CyanoPOX also has a conserved active site pocket when compared with mammalian lactoperoxidases. Due to its catalytic properties and high expression in a bacterial host, this newly discovered peroxidase shows promise for applications.

PubMed: 39570012
DOI: 10.1002/cbic.202400713

実験手法

X-RAY DIFFRACTION (1.74 Å)