The three zinc-containing alcohol dehydrogenases from baker's yeast,Saccharomyces cerevisiae

Abstract

This review is a summary of our current knowledge of the structure, function and mechanism of action of the three zinc-containing alcohol dehydrogenases, YADH-1, YADH-2 and YADH-3, in baker's yeast, Saccharomyces cerevisiae. The opening section deals with the substrate specificity of the enzymes, covering the steady-state kinetic data for its most known substrates. In the following sections, the kinetic mechanism for this enzyme is reported, along with the values of all rate constants in the mechanism. The complete primary structures of the three isoenzymes of YADH are given, and the model of the 3D structure of the active site is presented. All known artificial mutations in the primary structure of the YADH are covered in full and described in detail. Further, the chemical mechanism of action for YADH is presented along with the complement of steady-state and ligand-binding data supporting this mechanism. Finally, the bio-organic chemistry of the hydride-transfer reactions catalyzed by the enzyme is covered: this chemistry explains the narrow substrate specificity and the enantioselectivity of the yeast enzyme.

Effect of the size of yeast flocs and zinc supplementation on continuous ethanol fermentation performance and metabolic flux distribution under very high concentration conditions

“…It was proposed that the increase in the activity of ethanol dehydrogenase with zinc as a cofactor (Leskovac et al, 2002) accounts for enhanced ethanol production (Chandrasena and Walker, 1997). However, in the present work, it was found that there was no excretion of pyruvate, indicating that the enzymes controlling the pyruvate node could be enhanced by zinc supplementation and the pyruvate synthesized upstream might be metabolized quickly at the sub-nodes to the acetaldehyde and oxaloacetate pathways.…”

Beer with Reduced Ethanol Content Produced Using Saccharomyces cerevisiae Yeasts Deficient in Various Tricarboxylic Acid Cycle Enzymes

“…In the sample prepared with knocked-out ADH1, the ethanol content reached a value of 0.62% (v/v). However, this value, due to the presence of four other isoforms, may not be stable in other strains of brewing yeast with the same mutation 7 . Considerably higher concentrations of residual saccharides in the beer, or more generally high residual extract values, could pose a problem, but the presence of organic acids, such as lactate and citrate, has a protective effect against bacterial contamination.…”

Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example

“…The alcohol dehydrogenase lyophilized powder from Saccharomyces cerevisiae (Sigma-Aldrich A7011) (ADH) was used with no further purification. This enzyme has a molecular weight 141-151 kDa, an isoelectric point between 5.4-5.8 and the optimal pH is reported to be in the range of 8.6 and 9.0 [17][18][19].…”

“…The ADH (alcohol dehydrogenase) is a zinc-containing enzyme, usually used in the food industry [17]. The Saccharomyces cerevisiae produced three isoenzymes of alcohol dehydrogenase, YADH-1 (expressed during anaerobic fermentation), YADH-2 (cytoplasmic form repressed by glucose) and YADH-3 (found in mitochondria) [17].…”

“…The Saccharomyces cerevisiae produced three isoenzymes of alcohol dehydrogenase, YADH-1 (expressed during anaerobic fermentation), YADH-2 (cytoplasmic form repressed by glucose) and YADH-3 (found in mitochondria) [17]. ADH belongs to Alcohol: NAD + oxidoreductase class and structurally it is constituted by an asymmetric homotetramer with four different subunits, organized as analogous dimmers, (see in Fig.…”