Characterization of a New Glyoxal Oxidase from the Thermophilic Fungus Myceliophthora thermophila M77: Hydrogen Peroxide Production Retained in 5-Hydroxymethylfurfural Oxidation

被引：19

作者：

Seiki Kadowaki, Marco Antonio ^{[1
,2
,3
]}

de Godoy, Mariana Ortiz ^{[1
,2
,3
]}

Kumagai, Patricia Suemy ^{[1
]}

da Costa-Filho, Antonio Jose ^{[4
]}

Mort, Andrew ^{[2
,3
]}

Prade, Rolf Alexander ^{[2
,3
]}

Polikarpov, Igor ^{[1
]}

机构：

[1] Univ Sao Paulo, Sao Carlos Inst Phys, Av Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP, Brazil

[2] Oklahoma State Univ, Dept Biochem & Mol Biol, Stillwater, OK 74078 USA

[3] Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 USA

[4] Univ Sao Paulo, Ribeirao Preto Sch Philosophy Sci & Literature, Dept Phys, BR-14040901 Ribeirao Preto, Brazil

来源：

CATALYSTS | 2018年 / 8卷 / 10期

基金：

巴西圣保罗研究基金会;

关键词：

Myceliophthora; glyoxal oxidase; 5-hydroxymethylfurfural; PHANEROCHAETE-CHRYSOSPORIUM; GALACTOSE-OXIDASE; CRYSTAL-STRUCTURE; MOLECULAR-WEIGHT; PROTEINS; ENZYME; HYDROCARBONS; DEGRADATION; TRYPTOPHAN; RESOLUTION;

D O I：

10.3390/catal8100476

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Myceliophthora thermophyla is a thermophilic industrially relevant fungus that secretes an assortment of hydrolytic and oxidative enzymes for lignocellulose degradation. Among them is glyoxal oxidase (MtGLOx), an extracellular oxidoreductase that oxidizes several aldehydes and a-hydroxy carbonyl substrates coupled to the reduction of O-2 to H2O2. This copper metalloprotein belongs to a class of enzymes called radical copper oxidases (CRO) and to the "auxiliary activities" subfamily AA5_1 that is based on the Carbohydrate-Active enZYmes (CAZy) database. Only a few members of this family have been characterized to date. Here, we report the recombinant production, characterization, and structure-function analysis of MtGLOx. Electron Paramagnetic Resonance (EPR) spectroscopy confirmed MtGLOx to be a radical-coupled copper complex and small angle X-ray scattering (SAXS) revealed an extended spatial arrangement of the catalytic and four N-terminal WSC domains. Furthermore, we demonstrate that methylglyoxal and 5-hydroxymethylfurfural (HMF), a fermentation inhibitor, are substrates for the enzyme.

引用

页数：15