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Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation.
KADOWAKI, Marco Antonio Seiki; GODOY, Mariana Ortiz de; KUMAGAI, Patricia Suemy; COSTA FILHO, Antonio José da; MORT, Andrew; PRADE, Rolf Alexander; POLIKARPOV, Igor.
Abstract: 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 O2 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.
Catalysts
v. 8, n. 10, p. 476-1-476-15 - Ano: 2018
Fator de Impacto: 3,465
http://dx.doi.org/10.3390/catal8100476
    @article={002910739,author = {KADOWAKI, Marco Antonio Seiki; GODOY, Mariana Ortiz de; KUMAGAI, Patricia Suemy; COSTA FILHO, Antonio José da; MORT, Andrew; PRADE, Rolf Alexander; POLIKARPOV, Igor.},title={Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation},journal={Catalysts},note={v. 8, n. 10, p. 476-1-476-15},year={2018}}