8PHA
O(S)-methyltransferase from Pleurotus sapidus
Summary for 8PHA
| Entry DOI | 10.2210/pdb8pha/pdb |
| Descriptor | O-methyltransferase domain-containing protein, GLYCEROL, 2-HYDROXY BUTANE-1,4-DIOL, ... (6 entities in total) |
| Functional Keywords | biocatalysis, enzymes, fungi, o-methyltransferase, pleurotus sapidus, s-methyltransferase, transferase |
| Biological source | Pleurotus sapidus |
| Total number of polymer chains | 4 |
| Total formula weight | 215687.41 |
| Authors | Korf, L.,Essen, L.-O. (deposition date: 2023-06-19, release date: 2024-03-27, Last modification date: 2024-04-10) |
| Primary citation | Brescia, F.F.,Korf, L.,Essen, L.O.,Zorn, H.,Ruehl, M. A Novel O - and S -Methyltransferase from Pleurotus sapidus Is Involved in Flavor Formation. J.Agric.Food Chem., 72:6471-6480, 2024 Cited by PubMed Abstract: Increasing consumer aversion to non-natural flavoring substances is prompting a heightened interest in enzymatic processes for flavor production. This includes methylation reactions, which are often performed by using hazardous chemicals. By correlation of aroma profile data and transcriptomic analysis, a novel -methyltransferase (OMT) catalyzing a respective reaction within the formation of -anisaldehyde was identified in the mushroom . Heterologous expression in followed by purification allowed for further characterization of the enzyme. Besides -hydroxybenzaldehyde, the proposed precursor of -anisaldehyde, the enzyme catalyzed the methylation of further hydroxylated aromatic compounds at the - and -position. The values determined for -hydroxybenzaldehyde and -adenosyl-l-methionine were 80 and 107 μM, respectively. Surprisingly, the studied enzyme enabled the transmethylation of thiol-nucleophiles, as indicated by the formation of 2-methyl-3-(methylthio)furan from 2-methyl-3-furanthiol. Moreover, the enzyme was crystallized at a resolution of 2.0 Å, representing the first published crystal structure of a basidiomycetous OMT. PubMed: 38462720DOI: 10.1021/acs.jafc.3c08849 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
Download full validation report
