6QYI

Structure of HPAB from E.coli in complex with FAD

6QYI の概要

• エントリーDOI: 10.2210/pdb6qyi/pdb
• 分子名称: 4-hydroxyphenylacetate 3-monooxygenase oxygenase component, FLAVIN-ADENINE DINUCLEOTIDE, TRIETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: oxidoreductase monooxygenase, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121859.09

構造登録者

Pecqueur, L.,Lombard, M.,Deng, Y.,Fontecave, M. (登録日: 2019-03-09, 公開日: 2019-06-12, 最終更新日: 2024-05-15)

主引用文献

Deng, Y.,Faivre, B.,Back, O.,Lombard, M.,Pecqueur, L.,Fontecave, M.
Structural and Functional Characterization of 4-Hydroxyphenylacetate 3-Hydroxylase from Escherichia coli.
Chembiochem, 21:163-170, 2020

PubMed Abstract: The hydroxylation of phenols into polyphenols, which are valuable chemicals and pharmaceutical products, is a challenging reaction. The search for green synthetic processes has led to considering microorganisms and pure hydroxylases as catalysts for phenol hydroxylation. Herein, we report the structural and functional characterization of the flavin adenine dinucleotide (FAD)-dependent 4-hydroxyphenylacetate 3-monooxygenase from Escherichia coli, named HpaB. It is shown that this enzyme enjoys a relatively broad substrate specificity, which allows the conversion of a number of non-natural phenolic compounds, such as tyrosol, hydroxymandelic acid, coumaric acid, hydroxybenzoic acid and its methyl ester, and phenol, into the corresponding catechols. The reaction can be performed by using a simple chemical assay based on formate as the electron donor and the organometallic complex [Rh(bpy)Cp*(H O)] (Cp*: 1,2,3,4,5-pentamethylcyclopentadiene, bpy: 2,2'-bipyridyl) as the catalyst for FAD reduction. The availability of a crystal structure of HpaB in complex with FAD at 1.8 Å resolution opens up the possibility of the rational tuning of the substrate specificity and activity of this interesting class of phenol hydroxylases.

PubMed: 31155821
DOI: 10.1002/cbic.201900277

実験手法

X-RAY DIFFRACTION (1.8 Å)