Construction and optimization of a fungal secretion system suitable for high-yield...
| Full text | |
| 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 |