9GP0

4-allyl syringol oxidase from Streptomyces cavernae: complex with Vanillyl alcohol

9GP0 の概要

• エントリーDOI: 10.2210/pdb9gp0/pdb
• 分子名称: 4-allyl syringol oxidase from Streptomyces cavernae, FLAVIN-ADENINE DINUCLEOTIDE, 4-hydroxy-3-methoxybenzaldehyde, ... (4 entities in total)
• 機能のキーワード: fad, flavi, biocatalysis, oxidoreductase
• 由来する生物種: Streptomyces cavernae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123869.32

構造登録者

Mattevi, A.,Alvigini, L. (登録日: 2024-09-06, 公開日: 2025-02-05, 最終更新日: 2025-02-12)

主引用文献

Eggerichs, D.,Weddeling, H.G.,Alvigini, L.,Rapsch, T.,Weindorf, N.,Mattevi, A.,Tischler, D.
Kinetic and structural investigation of the 4-allyl syringol oxidase from Streptomyces cavernae.
Arch.Biochem.Biophys., 765:110320-110320, 2025

PubMed Abstract: 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), 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.

PubMed: 39870290
DOI: 10.1016/j.abb.2025.110320

実験手法

X-RAY DIFFRACTION (1.75 Å)