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 s), 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)