» Articles » PMID: 36009875

Thermostable and O-Insensitive Pyruvate Decarboxylases from Thermoacidophilic Archaea Catalyzing the Production of Acetaldehyde

Overview
Journal Biology (Basel)
Publisher MDPI
Specialty Biology
Date 2022 Aug 26
PMID 36009875
Authors
Affiliations
Soon will be listed here.
Abstract

Pyruvate decarboxylase (PDC) is a key enzyme involved in ethanol fermentation, and it catalyzes the decarboxylation of pyruvate to acetaldehyde and CO. Bifunctional PORs/PDCs that also have additional pyruvate:ferredoxin oxidoreductase (POR) activity are found in hyperthermophiles, and they are mostly oxygen-sensitive and CoA-dependent. Thermostable and oxygen-stable PDC activity is highly desirable for biotechnological applications. The enzymes from the thermoacidophiles (formerly ) (Ss, T = 80 °C) and (Sa, T = 80 °C) were purified and characterized, and their biophysical and biochemical properties were determined comparatively. Both enzymes were shown to be heterodimeric, and their two subunits were determined by SDS-PAGE to be 37 ± 3 kDa and 65 ± 2 kDa, respectively. The purified enzymes from and showed both PDC and POR activities which were CoA-dependent, and they were thermostable with half-life times of 2.9 ± 1 and 1.1 ± 1 h at 80 °C, respectively. There was no loss of activity in the presence of oxygen. Optimal pH values for their PDC and POR activity were determined to be 7.9 and 8.6, respectively. In conclusion, both thermostable SsPOR/PDC and SaPOR/PDC catalyze the CoA-dependent production of acetaldehyde from pyruvate in the presence of oxygen.

References
1.
Talarico L, Ingram L, Maupin-Furlow J . Production of the Gram-positive Sarcina ventriculi pyruvate decarboxylase in Escherichia coli. Microbiology (Reading). 2001; 147(Pt 9):2425-2435. DOI: 10.1099/00221287-147-9-2425. View

2.
Yan Z, Fushinobu S, Wakagi T . Four Cys residues in heterodimeric 2-oxoacid:ferredoxin oxidoreductase are required for CoA-dependent oxidative decarboxylation but not for a non-oxidative decarboxylation. Biochim Biophys Acta. 2014; 1844(4):736-43. DOI: 10.1016/j.bbapap.2014.01.015. View

3.
Schocke L, Brasen C, Siebers B . Thermoacidophilic Sulfolobus species as source for extremozymes and as novel archaeal platform organisms. Curr Opin Biotechnol. 2019; 59:71-77. DOI: 10.1016/j.copbio.2019.02.012. View

4.
Nunn C, Johnsen U, Schonheit P, Fuhrer T, Sauer U, Hough D . Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius. J Biol Chem. 2010; 285(44):33701-9. PMC: 2962468. DOI: 10.1074/jbc.M110.146332. View

5.
Iwasaki T, Wakagi T, Oshima T . Ferredoxin-dependent redox system of a thermoacidophilic archaeon, Sulfolobus sp. strain 7. Purification and characterization of a novel reduced ferredoxin-reoxidizing iron-sulfur flavoprotein. J Biol Chem. 1995; 270(30):17878-83. DOI: 10.1074/jbc.270.30.17878. View