9H40
Pinoresinol hydroxylase from Pseudomonas sp.
Summary for 9H40
| Entry DOI | 10.2210/pdb9h40/pdb |
| Descriptor | p-cresol methylhydroxylase, ALANINE, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | fad, flavin, dehydrogenase, alcohol, enzyme mechanism, flavoprotein |
| Biological source | Pseudomonas sp. |
| Total number of polymer chains | 2 |
| Total formula weight | 126757.39 |
| Authors | |
| Primary citation | Guerriere, T.B.,Fraaije, M.W.,Mattevi, A. Biochemical and structural insights into pinoresinol hydroxylase from Pseudomonas sp. Arch.Biochem.Biophys., 764:110247-110247, 2024 Cited by PubMed Abstract: The vanillyl alcohol oxidase/p-cresol methylhydroxylase (VAO/PCMH) flavoprotein family comprises a broad spectrum of enzymes capable of catalyzing the oxidative bioconversions of various substrates. Among them, pinoresinol hydroxylase (PinH) from the 4-alkylphenol oxidizing subgroup initiates the oxidative degradation of (+)-pinoresinol, a lignan important for both lignin structure and plant defense. In this study, we present a detailed biochemical and structural characterization of PinH from Pseudomonas sp., with focus on its substrate specificity and product formation. PinH was expressed in E. coli and purified as FAD-containing, soluble protein. The flavoenzyme catalyzes the hydroxylation of both (+)-pinoresinol and eugenol. Structural analysis reveals its dimeric form, non-covalent flavin binding, and a large active site. AlphaFold models of the PinH-cytochrome complex demonstrate cytochrome's dual role in electron transfer and modulating PinH's conformation. A distinctive feature of PinH is a large cavity that hosts its multi-ring (+)-pinoresinol substrate. The capability of converting bulky lignans is particularly attractive for biotechnological applications aimed at producing high-value compounds from phenolic precursors. These insights expand our knowledge on the structure and mechanism of the VAO/PCMH flavoenzyme family members. PubMed: 39613284DOI: 10.1016/j.abb.2024.110247 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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