Yeast alcohol dehydrogenase activation

Yang, R and Russell, A. 1., Optimization of baker s yeast alcohol dehydrogenase activity in an organic solvent, BiotechnoL Prog., 9, 234—241, 1993. 

Yeast alcohol dehydrogenase, 5. 1009 cobalt-containing, 5, 1013 manganese-containing, S, 1014 Yeast enolase activation... 

Blandino, A., Caro, I., and Cantero, D. (1997). Comparative study of alcohol dehydrogenase activity in flor yeast extracts. Biotechnol. Lett. 19, 651-654. 

Twu, J.S., Wold, F. (1973). Butyl isocyanate and active site specific reagent for yeast alcohol dehydrogenase. Biochemistry 12 381-6. 

The interaction of yeast alcohol dehydrogenase, zinc, and DPN to form the active holoenzyme is therefore indicated as follows ... 

Yeast alcohol dehydrogenase was crystallized from brewer s yeast by Negelein and Wulff (1937) and found to be dependent upon DPN for its activity by Anderson (1934). A distinctly different alcohol dehydrogenase was crystallized from horse liver by Bonnichsen and Wass6n (1948) and Bonnichsen (1950). The present discussion will be concerned primarily with those structural and functional aspects of the yeast enzyme which... 

The results of cysteine modification confirm the similarities in structure and function of the active sites of mammalian and yeast alcohol dehydrogenases (Section II,D). Minor differences are, however, observed. Thus, the nicotinamide-substituted imidazole dinucleotide (137) selectively alkylates one of the two cysteine ligands to the catalytic zinc atom, Cys-43, in the yeast enzyme. In the horse enzyme, on the other hand, the same reagent alkylates a different ligand to the same zinc atom, Cys-174. 

The auxin-Hke activity of benzo[ft]selenienyl-3-acetic acid has been confirmed <83P2657,85M1 213-06>. The phototoxicity of a-terthienyl is claimed to be higher against yeast alcohol dehydrogenase than a-terselenienyl <84Ml 2l3-03>. 

Yeast alcohol dehydrogenase (ADH) has its highest activity at 30°, and this decreases sharply with increase of temperature above 50°. No activity is observed at 70°. This inactivation process can be monitored by measuring the remaining activity of the enzyme during the incubation at elevated temperatures. ADH from yeast is assayed by monitoring ethanol-dependent NAD reduction at 340 nm ADH activity is expressed as micromoles of NADH produced per minute with a molar absorption coefficient of 6.22 mA/ cm . The influence of molecular chaperonin on ADH inactivation can be examined as follows. 

---