Nicotinamide adenine dinucleotide dehydrogenase yeast

Kirschner, K., Eigen, M., Bittman, R. Voigt, B. (1966). The binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde 3-phosphate dehydrogenase temperature jump relaxation studies on the mechanism of an allosteric enzyme. Proceedings of the National Academy of Sciences, USA, 56, 1661-7. 

We shall start the discussion with a classical experiment related to the stereochemistry of oxidation of ethanol and reduction of acetaldehyde mediated by the enzyme yeast alcohol dehydrogenase in the presence of the oxidized (NAD+) and reduced (NADH) forms, respectively, of the coenzyme nicotinamide adenine dinucleotide (Fig. 54). The stereochemically interesting feature of this reaction stems from the fact that the methylene hydrogens in CH3CH2OH and the faces of the carbonyl in CH3CH = 0 are enantiotopic. The question thus arises which of the CH2-hydrogens... 

Scheme 1.—The Reactions Involved in the Enzymic Determination of (a) Glycerol, (b) Erythritol, (c) Glycolaldehyde, and (d) and (e) Formic Acid. [Abbreviations ATP, adenosine 5 -triphosphate ADP, adenosine S -pyrophosphate NAD and NADH, the oxidized and reduced forms of nicotinamide adenine dinucleotide PEP, enolpyruvate phosphate Pi, inorganic orthophosphate GK, glycerol kinase GDH, u-glycerophosphate dehydrogenase EK, erythritol kinase PK, pyruvate kinase YAD, yeast alcohol dehydrogenase FS, formyltetrahydrofolate synthetase FD, formate dehydrogenase and NR, nitrate reductase.]...

Alcohol dehydrogenase is one of the active enzymes in yeast. The active site in alcohol dehydrogenase contains a zinc ion, Zn, that is coordinated to the sulfur atoms of two cysteine residues of the enzyme. The hydride reducing reagent in alcohol dehydrogenase is nicotinamide adenine dinucleotide, NADH, which transfers a hydride ion to a carbonyl compound to yield an alcohol and NAD" ", in a mechanism that is related to the Cannizzaro reaction (Sec. 16.3). 

The example of the reversible oxidation of ethanol (CH3CH2OH) to ethanal (acetaldehyde, CH3CHO) by yeast alcohol dehydrogenase (alcohol NAD " oxidore-ductase [EC 1.1.1.1]) is one such (now classical) process and is discussed below. The oxidoreductase uses nicotinamide adenine dinucleotide (NAD") (oxidized form) as its coenzyme, and it is in the pyridine (azabenzene, C5H5N) ring that the reduction is clearly seen. 

As another example, studies with deuterium-labeled substrates have shown that the reaction of ethanol with the coenzyme nicotinamide adenine dinucleotide (NAD+) catalyzed by yeast alcohol dehydrogenase occurs with exclusive removal of the pro-R hydrogen from ethanol and with addition only to the Re face of NAD" ". 

There are, however, many enzymes which, because they do not seem to be contained in such cellular particles, are referred to as soluble enzymes . Thus, the chemical reactions whereby the yeast cell converts glucose into ethanol and which seem to be identical with the first sequence of reactions in the normal respiration of plant cells are catalysed by such soluble enzymes. In the living cell such enzymes may, however, function as an organised multi-enzyme system which forms part of the endoplasmic reticulum. The fact that they cannot be obtained in association may merely reflect our inability to preserve the endoplasmic reticulum in cell-free preparations. Thus, in alcoholic fermentation by the yeast cell, which occurs in the absence of oxygen, there is an oxidative reaction which is balanced by a reduction. These both involve dehydrogenase enzymes having the same co-enzyme, nicotinamide adenine dinucleotide. One of these reactions, that catalysed by alcohol dehydrogenase, has already been mentioned (p. 73, eqn. 6). The other reaction... 

Nicotinamide l,iV -ethenoadenine dinucleotide, prepared from NAD+ and chloroacetaldehyde, has been converted into 3-aminopyridine l,A -etheno-adenine dinucleotide (4) by a pyridine base exchange reaction which was catalysed by the venom of Bungarus fasciatus. Yeast alcohol dehydrogenase was... 

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