2VAO

STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH ISOEUGENOL

2VAO の概要

• エントリーDOI: 10.2210/pdb2vao/pdb
• 分子名称: VANILLYL-ALCOHOL OXIDASE, FLAVIN-ADENINE DINUCLEOTIDE, 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol, ... (4 entities in total)
• 機能のキーワード: flavoenzyme, oxidase, catalysis
• 由来する生物種: Penicillium simplicissimum
• 細胞内の位置: Peroxisome: P56216
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 128113.74

構造登録者

Mattevi, A. (登録日: 1997-04-10, 公開日: 1997-10-15, 最終更新日: 2024-10-23)

主引用文献

Mattevi, A.,Fraaije, M.W.,Mozzarelli, A.,Olivi, L.,Coda, A.,van Berkel, W.J.
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
Structure, 5:907-920, 1997

PubMed Abstract: Lignin degradation leads to the formation of a broad spectrum of aromatic molecules that can be used by various fungal micro-organisms as their sole source of carbon. When grown on phenolic compounds, Penicillium simplicissimum induces the strong impression of a flavin-containing vanillyl-alcohol oxidase (VAO). The enzyme catalyses the oxidation of a vast array of substrates, ranging from aromatic amines to 4-alkyphenols. VAO is a member of a novel class of widely distributed oxidoreductases, which use flavin adenine dinucleotide (FAD) as a cofactor covalently bound to the protein. We have carried out the determination of the structure of VAO in order to shed light on the most interesting features of these novel oxidoreductases, such as the functional significance of covalent flavinylation and the mechanism of catalysis.

PubMed: 9261083
DOI: 10.1016/S0969-2126(97)00245-1

実験手法

X-RAY DIFFRACTION (2.8 Å)