6O9N

Structural insights on a new fungal aryl-alcohol oxidase

6O9N の概要

• エントリーDOI: 10.2210/pdb6o9n/pdb
• 分子名称: Aryl-alcohol oxidase, TRIS-HYDROXYMETHYL-METHYL-AMMONIUM, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• 機能のキーワード: aryl-alcohol oxidase aa3 family myceliophthora thermophila, oxidoreductase
• 由来する生物種: Myceliophthora thermophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 143392.41

構造登録者

Kadowaki, M.A.S.,Polikarpov, I. (登録日: 2019-03-14, 公開日: 2020-03-18, 最終更新日: 2024-11-20)

主引用文献

Kadowaki, M.A.S.,Higasi, P.M.R.,de Godoy, M.O.,de Araujo, E.A.,Godoy, A.S.,Prade, R.A.,Polikarpov, I.
Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77.
Biochim Biophys Acta Gen Subj, 1864:129681-129681, 2020

PubMed Abstract: Background Fungal aryl-alcohol oxidases (AAOx) are extracellular flavoenzymes that belong to glucose-methanol-choline oxidoreductase family and are responsible for the selective conversion of primary aromatic alcohols into aldehydes and aromatic aldehydes to their corresponding acids, with concomitant production of hydrogen peroxide (HO) as by-product. The HO can be provided to lignin degradation pathway, a biotechnological property explored in biofuel production. In the thermophilic fungus Thermothelomyces thermophilus (formerly Myceliophthora thermophila), just one AAOx was identified in the exo-proteome. Methods The glycosylated and non-refolded crystal structure of an AAOx from T. thermophilus at 2.6 Å resolution was elucidated by X-ray crystallography combined with small-angle X-ray scattering (SAXS) studies. Moreover, biochemical analyses were carried out to shed light on enzyme substrate specificity and thermostability. Results This flavoenzyme harbors a flavin adenine dinucleotide as a cofactor and is able to oxidize aromatic substrates and 5-HMF. Our results also show that the enzyme has similar oxidation rates for bulky or simple aromatic substrates such as cinnamyl and veratryl alcohols. Moreover, the crystal structure of MtAAOx reveals an open active site, which might explain observed specificity of the enzyme. Conclusions MtAAOx shows previously undescribed structural differences such as a fully accessible catalytic tunnel, heavy glycosylation and Ca binding site providing evidences for thermostability and activity of the enzymes from AA3_2 subfamily. General significance Structural and biochemical analyses of MtAAOx could be important for comprehension of aryl-alcohol oxidases structure-function relationships and provide additional molecular tools to be used in future biotechnological applications.

PubMed: 32653619
DOI: 10.1016/j.bbagen.2020.129681

実験手法

X-RAY DIFFRACTION (2.598 Å)