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

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

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GÓMEZ-MANZO, Saúl, José E. ESCAMILLA, Abigail GONZÁLEZ-VALDEZ, Gabriel LÓPEZ-VELÁZQUEZ, América VANOYE-CARLO, Jaime MARCIAL-QUINO, Ignacio DE LA MORA-DE LA MORA, Itzhel GARCIA-TORRES, Sergio ENRÍQUEZ-FLORES, Martha Lucinda CONTRERAS-ZENTELLA, Roberto ARREGUÍN-ESPINOSA, Peter M. H. KRONECK, Martha Elena SOSA-TORRES, 2015. The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme : Alcohol-Aldehyde Dehydrogenase (ADHa). In: International Journal of Molecular Sciences. 16(1), pp. 1293-1311. eISSN 1422-0067

@article{Gomez-Manzo2015Oxida-31144, title={The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme : Alcohol-Aldehyde Dehydrogenase (ADHa)}, year={2015}, doi={10.3390/ijms16011293}, number={1}, volume={16}, journal={International Journal of Molecular Sciences}, pages={1293--1311}, author={Gómez-Manzo, Saúl and Escamilla, José E. and González-Valdez, Abigail and López-Velázquez, Gabriel and Vanoye-Carlo, América and Marcial-Quino, Jaime and de la Mora-de la Mora, Ignacio and Garcia-Torres, Itzhel and Enríquez-Flores, Sergio and Contreras-Zentella, Martha Lucinda and Arreguín-Espinosa, Roberto and Kroneck, Peter M. H. and Sosa-Torres, Martha Elena} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/31144"> <dc:contributor>Marcial-Quino, Jaime</dc:contributor> <dc:creator>Escamilla, José E.</dc:creator> <dc:contributor>López-Velázquez, Gabriel</dc:contributor> <dc:contributor>Escamilla, José E.</dc:contributor> <dc:contributor>Gómez-Manzo, Saúl</dc:contributor> <dc:language>eng</dc:language> <dc:contributor>Vanoye-Carlo, América</dc:contributor> <dc:creator>Vanoye-Carlo, América</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-06-12T08:25:16Z</dc:date> <dc:creator>de la Mora-de la Mora, Ignacio</dc:creator> <dc:contributor>de la Mora-de la Mora, Ignacio</dc:contributor> <dc:creator>Garcia-Torres, Itzhel</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.de/urn:nbn:de:bsz:352-20150305140228786-3747162-5"/> <dc:creator>Gómez-Manzo, Saúl</dc:creator> <dc:creator>González-Valdez, Abigail</dc:creator> <dc:creator>Enríquez-Flores, Sergio</dc:creator> <dc:creator>Sosa-Torres, Martha Elena</dc:creator> <dc:contributor>Sosa-Torres, Martha Elena</dc:contributor> <dc:creator>Arreguín-Espinosa, Roberto</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-06-12T08:25:16Z</dcterms:available> <dc:contributor>González-Valdez, Abigail</dc:contributor> <dcterms:title>The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme : Alcohol-Aldehyde Dehydrogenase (ADHa)</dcterms:title> <dcterms:issued>2015</dcterms:issued> <dc:creator>Marcial-Quino, Jaime</dc:creator> <dc:creator>López-Velázquez, Gabriel</dc:creator> <dc:contributor>Contreras-Zentella, Martha Lucinda</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/31144"/> <dcterms:abstract xml:lang="eng">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.</dcterms:abstract> <dc:contributor>Enríquez-Flores, Sergio</dc:contributor> <dc:contributor>Arreguín-Espinosa, Roberto</dc:contributor> <dc:creator>Contreras-Zentella, Martha Lucinda</dc:creator> <dc:creator>Kroneck, Peter M. H.</dc:creator> <dc:contributor>Kroneck, Peter M. H.</dc:contributor> <dc:contributor>Garcia-Torres, Itzhel</dc:contributor> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 12.06.2015 (Informationen über die Zugriffsstatistik)

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