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...
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| Veröffentlicht in: | International journal of molecular sciences 2015-01, Vol.16 (1), p.1293-1311 |
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| creator | 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 |
| description | 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. |
| doi_str_mv | 10.3390/ijms16011293 |
| format | Article |
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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.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms16011293</identifier><identifier>PMID: 25574602</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>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</subject><ispartof>International journal of molecular sciences, 2015-01, Vol.16 (1), p.1293-1311</ispartof><rights>Copyright MDPI AG 2015</rights><rights>2015 by the authors; licensee MDPI, Basel, Switzerland. 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-a767c01ffaf89ddf716e314b7a69a2d9bbb9c63e3caec04a40361a0dca74071e3</citedby><cites>FETCH-LOGICAL-c511t-a767c01ffaf89ddf716e314b7a69a2d9bbb9c63e3caec04a40361a0dca74071e3</cites><orcidid>0000-0003-2095-9182 ; 0000-0002-4611-4770</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4307304/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4307304/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25574602$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gómez-Manzo, Saúl</creatorcontrib><creatorcontrib>Escamilla, José E</creatorcontrib><creatorcontrib>González-Valdez, Abigail</creatorcontrib><creatorcontrib>López-Velázquez, Gabriel</creatorcontrib><creatorcontrib>Vanoye-Carlo, América</creatorcontrib><creatorcontrib>Marcial-Quino, Jaime</creatorcontrib><creatorcontrib>de la Mora-de la Mora, Ignacio</creatorcontrib><creatorcontrib>Garcia-Torres, Itzhel</creatorcontrib><creatorcontrib>Enríquez-Flores, Sergio</creatorcontrib><creatorcontrib>Contreras-Zentella, Martha Lucinda</creatorcontrib><creatorcontrib>Arreguín-Espinosa, Roberto</creatorcontrib><creatorcontrib>Kroneck, Peter M H</creatorcontrib><creatorcontrib>Sosa-Torres, Martha Elena</creatorcontrib><title>The oxidative fermentation of ethanol in Gluconacetobacter diazotrophicus is a two-step pathway catalyzed by a single enzyme: alcohol-aldehyde Dehydrogenase (ADHa)</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>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.</description><subject>Acetates - analysis</subject><subject>Alcohol Dehydrogenase - chemistry</subject><subject>Alcohol Dehydrogenase - isolation & purification</subject><subject>Alcohol Dehydrogenase - metabolism</subject><subject>Aldehydes - analysis</subject><subject>Amino Acid Sequence</subject><subject>Biocatalysis</subject><subject>Carbon Radioisotopes - chemistry</subject><subject>Catalysts</subject><subject>Dehydrogenases</subject><subject>Enzyme kinetics</subject><subject>Enzymes</subject><subject>Ethanol - metabolism</subject><subject>Fermentation</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>Gluconacetobacter - enzymology</subject><subject>Gluconacetobacter diazotrophicus</subject><subject>Isotope Labeling</subject><subject>Kinetics</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Sequence Data</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Protein Denaturation</subject><subject>Temperature</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkk1v1DAQhiMEomXhxhlZ4lIkAv5KTDggVS20SJW4lHM0cSYbrxx7sZ2W7N_hj-JVS7Vw4TQzmkfvfOgtipeMvhOioe_NZoqspozxRjwqjpnkvKS0Vo8P8qPiWYwbSrngVfO0OOJVpWRN-XHx63pE4n-aHpK5QTJgmNClXHhH_EAwjeC8JcaRCztr70Bj8h3ohIH0BnY-Bb8djZ4jMZEASbe-jAm3ZAtpvIWFaEhglx32pFtyPxq3tkjQ7ZYJPxKw2o_elmB7HJceyfk-BL9GBxHJyen5Jbx5XjwZwEZ8cR9Xxfcvn6_PLsurbxdfz06vSl0xlkpQtdKUDQMMH5q-HxSrUTDZKagb4H3TdV2ja4FCA2oqQVJRM6C9BiWpYihWxac73e3cTdjr_IgAtt0GM0FYWg-m_bvjzNiu_U0rBVWCyixwci8Q_I8ZY2onEzVaCw79HFumeN6RiTz5v2gtK84bqfbo63_QjZ-Dy5_IVL68YSyPXxVv7ygdfIwBh4e9GW33RmkPjZLxV4e3PsB_nCF-A9WdvXI</recordid><startdate>20150107</startdate><enddate>20150107</enddate><creator>Gómez-Manzo, Saúl</creator><creator>Escamilla, José E</creator><creator>González-Valdez, Abigail</creator><creator>López-Velázquez, Gabriel</creator><creator>Vanoye-Carlo, América</creator><creator>Marcial-Quino, Jaime</creator><creator>de la Mora-de la Mora, Ignacio</creator><creator>Garcia-Torres, Itzhel</creator><creator>Enríquez-Flores, Sergio</creator><creator>Contreras-Zentella, Martha Lucinda</creator><creator>Arreguín-Espinosa, Roberto</creator><creator>Kroneck, Peter M H</creator><creator>Sosa-Torres, Martha Elena</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QL</scope><scope>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-2095-9182</orcidid><orcidid>https://orcid.org/0000-0002-4611-4770</orcidid></search><sort><creationdate>20150107</creationdate><title>The oxidative fermentation of ethanol in Gluconacetobacter diazotrophicus is a two-step pathway catalyzed by a single enzyme: alcohol-aldehyde Dehydrogenase (ADHa)</title><author>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</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-a767c01ffaf89ddf716e314b7a69a2d9bbb9c63e3caec04a40361a0dca74071e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Acetates - 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Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gómez-Manzo, Saúl</au><au>Escamilla, José E</au><au>González-Valdez, Abigail</au><au>López-Velázquez, Gabriel</au><au>Vanoye-Carlo, América</au><au>Marcial-Quino, Jaime</au><au>de la Mora-de la Mora, Ignacio</au><au>Garcia-Torres, Itzhel</au><au>Enríquez-Flores, Sergio</au><au>Contreras-Zentella, Martha Lucinda</au><au>Arreguín-Espinosa, Roberto</au><au>Kroneck, Peter M H</au><au>Sosa-Torres, Martha Elena</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The oxidative fermentation of ethanol in Gluconacetobacter diazotrophicus is a two-step pathway catalyzed by a single enzyme: alcohol-aldehyde Dehydrogenase (ADHa)</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2015-01-07</date><risdate>2015</risdate><volume>16</volume><issue>1</issue><spage>1293</spage><epage>1311</epage><pages>1293-1311</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><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.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>25574602</pmid><doi>10.3390/ijms16011293</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0003-2095-9182</orcidid><orcidid>https://orcid.org/0000-0002-4611-4770</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; MDPI - Multidisciplinary Digital Publishing Institute; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| 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 |
| title | 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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