9goz | pdb_00009goz

4-Allyl syringol oxidase from Streptomyces cavernae: complex with eugenol

spinqualitylabelsall models 9goz, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9goz is a 2 chain structure with sequence from Streptomyces cavernae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: EOL, FAD, P4G, P6G, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 4-Phenol oxidases are proposed to be involved in the utilization of lignin-derived aromatic compounds. While enzymes with selectivity towards 4-hydroxyphenyl and guaiacyl motifs are well described, we identified the first syringyl-specific oxidase from Streptomyces cavernae (Sc4ASO) only very recently. Here, in-depth studies were conducted to unravel the molecular origins of the outstanding selectivity of Sc4ASO. Kinetic experiments revealed high activities on dimethoxylated substrates (up to 2.9 +/- 0.1 s(-1)), but also strong cooperativity between both protein subunits, as well as substrate inhibition in dependency of ortho methoxylation and chain length of the para substituent. Rapid mixing kinetics in combination with the determination of the crystal structure in complex with three substrates allowed to connect the kinetic behavior with never-observed positioning of the conserved residue Y471. Ultimately, the catalytic potential of Sc4ASO was investigated in a 100 mL scale cascade reaction to produce the natural product syringaresinol. Kinetic and structural investigation of the 4-allyl syringol oxidase from Streptomyces cavernae.,Eggerichs D, Weddeling HG, Alvigini L, Rapsch T, Weindorf N, Mattevi A, Tischler D Arch Biochem Biophys. 2025 Jan 25;765:110320. doi: 10.1016/j.abb.2025.110320. PMID:39870290 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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