8S6C
Crystal structure of Cyanobacterium TDX16 peroxidase
Summary for 8S6C
| Entry DOI | 10.2210/pdb8s6c/pdb |
| Descriptor | Lactoperoxidase, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | heme, oxidoreductase |
| Biological source | cyanobacterium TDX16 |
| Total number of polymer chains | 1 |
| Total formula weight | 57638.13 |
| Authors | Rozeboom, H.J.,Savino, S.,Fraaije, M.W. (deposition date: 2024-02-27, release date: 2024-12-04, Last modification date: 2025-02-05) |
| Primary citation | 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 Cited by 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: 39570012DOI: 10.1002/cbic.202400713 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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