8S1J
Crystal structure of t-anethole oxygenase from Stenotrophomonas maltophilia
Summary for 8S1J
| Entry DOI | 10.2210/pdb8s1j/pdb |
| Descriptor | Trans-anethole oxygenase, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | oxygenase, c=c cleavage, bacterial, heme, oxidoreductase |
| Biological source | Stenotrophomonas maltophilia |
| Total number of polymer chains | 2 |
| Total formula weight | 72077.79 |
| Authors | |
| Primary citation | Purwani, N.N.,Rozeboom, H.J.,Willers, V.P.,Wijma, H.J.,Fraaije, M.W. Discovery of a new class of bacterial heme-containing CC cleaving oxygenases. N Biotechnol, 83:82-90, 2024 Cited by PubMed Abstract: Previously, some bacteria were shown to harbour enzymes capable of catalysing the oxidative cleavage of the double bond of t-anethole and related compounds. The cofactor dependence of these enzymes remained enigmatic due to a lack of biochemical information. We report on catalytic and structural details of a representative of this group of oxidative enzymes: t-anethole oxygenase from Stenotrophomonas maltophilia (TAO). The bacterial enzyme could be recombinantly expressed and purified, enabling a detailed biochemical study that has settled the dispute on its cofactor dependence. We have established that TAO contains a tightly bound b-type heme and merely depends on dioxygen for catalysis. It was found to accept t-anethole, isoeugenol and O-methyl isoeugenol as substrates, all being converted into the corresponding aromatic aldehydes without the need of any cofactor regeneration. The elucidated crystal structure of TAO has revealed that it contains a unique active site architecture that is conserved for this distinct class of heme-containing bacterial oxygenases. Similar to other hemoproteins, TAO has a histidine (His121) as proximal ligand. Yet, unique for TAOs, an arginine (Arg89) is located at the distal axial position. Site directed mutagenesis confirmed crucial roles for these heme-liganding residues and other residues that form the substrate binding pocket. In conclusion, the results reported here reveal a new class of bacterial heme-containing oxygenases that can be used for the cleavage of alkene double bonds, analogous to ozonolysis in organic chemistry. PubMed: 39053683DOI: 10.1016/j.nbt.2024.07.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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