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Int. J. Mol. Sci. 2015, 16(1), 1293-1311; doi:10.3390/ijms16011293

The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme: Alcohol-Aldehyde Dehydrogenase (ADHa)

1
Laboratorio de Bioquímica-Genética, Instituto Nacional de Pediatría, S.S. Mexico City 04530, Mexico
2
Departamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico
3
Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico
4
Coordinación de Investigación, Facultad de Medicina, Universidad La Salle, Mexico City 14000, Mexico
5
CONACyT, Comisionado a Instituto Nacional de Pediatría, S.S. Mexico City 03940, Mexico
6
Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior s/n, Ciudad Universitaria, Mexico City 04510, Mexico
7
Fachbereich Biologie, Universität Konstanz, 78457 Konstanz, Germany
8
Departamento de Química Inorgánica y Nuclear, Facultad de Química, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico
This work is dedicated to Prof. Jos
*
Authors to whom correspondence should be addressed.
Academic Editor: Ulf Hanefeld
Received: 30 October 2014 / Accepted: 15 December 2014 / Published: 7 January 2015
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [3051 KB, uploaded 7 January 2015]   |  

Abstract

Gluconacetobacter diazotrophicus is a N2-fixing bacterium endophyte from sugar cane. The oxidation of ethanol to acetic acid of this organism takes place in the periplasmic space, and this reaction is catalyzed by two membrane-bound enzymes complexes: the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase (ALDH). We present strong evidence showing that the well-known membrane-bound Alcohol dehydrogenase (ADHa) of Ga. diazotrophicus is indeed a double function enzyme, which is able to use primary alcohols (C2–C6) and its respective aldehydes as alternate substrates. Moreover, the enzyme utilizes ethanol as a substrate in a reaction mechanism where this is subjected to a two-step oxidation process to produce acetic acid without releasing the acetaldehyde intermediary to the media. Moreover, we propose a mechanism that, under physiological conditions, might permit a massive conversion of ethanol to acetic acid, as usually occurs in the acetic acid bacteria, but without the transient accumulation of the highly toxic acetaldehyde. View Full-Text
Keywords: bifunctional enzyme-active alcohol dehydrogenase (ADHa); ethanol-acetaldehyde-oxidation; Gluconacetobacter diazotrophicus; acetic acid bacteria; alcohol aldehyde dehydrogenase bifunctional enzyme-active alcohol dehydrogenase (ADHa); ethanol-acetaldehyde-oxidation; Gluconacetobacter diazotrophicus; acetic acid bacteria; alcohol aldehyde dehydrogenase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Gómez-Manzo, S.; Escamilla, J.E.; González-Valdez, A.; López-Velázquez, G.; Vanoye-Carlo, A.; Marcial-Quino, J.; de la Mora-de la Mora, I.; Garcia-Torres, I.; Enríquez-Flores, S.; Contreras-Zentella, M.L.; Arreguín-Espinosa, R.; Kroneck, P.M.H.; Sosa-Torres, M.E. The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme: Alcohol-Aldehyde Dehydrogenase (ADHa). Int. J. Mol. Sci. 2015, 16, 1293-1311.

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