The oxidative fermentation of ethanol in Gluconacetobacter diazotrophicus is a two-step pathway catalyzed by a single enzyme: alcohol-aldehyde Dehydrogenase (ADHa)

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...

Full description

Saved in:
Bibliographic Details
Published in:International journal of molecular sciences 2015-01, Vol.16 (1), p.1293-1311
Main Authors: Gómez-Manzo, Saúl, Escamilla, José E, González-Valdez, Abigail, López-Velázquez, Gabriel, Vanoye-Carlo, América, Marcial-Quino, Jaime, de la Mora-de la Mora, Ignacio, Garcia-Torres, Itzhel, Enríquez-Flores, Sergio, Contreras-Zentella, Martha Lucinda, Arreguín-Espinosa, Roberto, Kroneck, Peter M H, Sosa-Torres, Martha Elena
Format: Article
Language:English
Subjects:
Acetates - analysis
Alcohol Dehydrogenase - chemistry
Alcohol Dehydrogenase - isolation & purification
Alcohol Dehydrogenase - metabolism
Aldehydes - analysis
Amino Acid Sequence
Biocatalysis
Carbon Radioisotopes - chemistry
Catalysts
Dehydrogenases
Enzyme kinetics
Enzymes
Ethanol - metabolism
Fermentation
Gas Chromatography-Mass Spectrometry
Gluconacetobacter - enzymology
Gluconacetobacter diazotrophicus
Isotope Labeling
Kinetics
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Oxidation
Oxidation-Reduction
Protein Denaturation
Temperature
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms16011293