The oxidative fermentation of ethanol in Gluconacetobacter diazotrophicus is a two-step pathway catalyzed by a single enzyme: alcohol-aldehyde dehydrogenase (ADHa)
메타 데이터
바이오화학분류
바이오플라스틱
플라스틱
바이오정밀화학
용매
화학제품
연료
화장품용 기능성소재
계면활성제⁄증점제
의료용 화학소재
식품첨가제
논문
The oxidative fermentation of ethanol in Gluconacetobacter diazotrophicus is a two-step pathway catalyzed by a single enzyme: alcohol-aldehyde dehydrogenase (ADHa)
학술지
International journal of molecular sciences
저자명
Gó mez-Manzo, Saú l; Escamilla, José E.; Gonzá lez-Valdez, Abigail; Ló pez-Velá zquez, Gabriel; Vanoye-Carlo, Amé rica; Marcial-Quino, Jaime; de la Mora-de la Mora, Ignacio; Garcia-Torres, Itzhel; Enrí quez-Flores, Sergio; Contreras-Zentella, Martha Lucinda; Arreguí n-Espinosa, Roberto; Kroneck, Peter M. H.; Sosa-Torres, Martha Elena
초록
<P><I>Gluconacetobacter diazotrophicus</I> is a N<SUB>2</SUB>-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 <I>Ga. diazotrophicus</I> 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.</P>