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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Seiki Kadowaki, Marco Antonio [1, 2, 3] ; de Godoy, Mariana Ortiz [1, 2, 3] ; Kumagai, Patricia Suemy [3] ; da Costa-Filho, Antonio Jose [4] ; Mort, Andrew [1, 2] ; Prade, Rolf Alexander [1, 2] ; Polikarpov, Igor [3]
Total Authors: 7
Affiliation:
[1] Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 - USA
[2] Oklahoma State Univ, Dept Biochem & Mol Biol, Stillwater, OK 74078 - USA
[3] Univ Sao Paulo, Sao Carlos Inst Phys, Av Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil
[4] Univ Sao Paulo, Ribeirao Preto Sch Philosophy Sci & Literature, Dept Phys, BR-14040901 Ribeirao Preto - Brazil
Total Affiliations: 4
Document type: Journal article
Source: CATALYSTS; v. 8, n. 10 OCT 2018.
Web of Science Citations: 0
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 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. (AU)

FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants
FAPESP's process: 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis
Grantee:Marco Antonio Seiki Kadowaki
Support type: Scholarships in Brazil - Post-Doctorate