| Autor: |
Saúl Gómez-Manzo, 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 |
| Jazyk: |
angličtina |
| Rok vydání: |
2015 |
| Předmět: |
|
| Zdroj: |
International Journal of Molecular Sciences, Vol 16, Iss 1, Pp 1293-1311 (2015) |
| Druh dokumentu: |
article |
| ISSN: |
1422-0067 |
| DOI: |
10.3390/ijms16011293 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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