Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An efficient procedure for the purification of yeast alcohol dehydrogenase I (ADHI) was developed. By using Blue-Sepharose 4B affinity chromatography, ADHI from yeast (S. cerevisiae) was purified 200-fold with an overall yield of 47% to homogeneity as judged by sodium dodecyl sulfate polyacrylamide gel electrophoresis and starch gel electrophoresis. Results of studies on the product and dead-end inhibition kinetics were in agreement with and ordered Bi Bi mechanism as proposed by Wratten and Cleland. Dioxane was found to be a competitive inhibitor of this enzyme. The complexity of the reaction mechanism of this enzyme is discussed.
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PMID:Purification and Kinetic Studies of Yeast Alcohol Dehydrogenase I. 1223 32

Using a modification of the basic two-dimensional polyacrylamide gel electrophoresis technique, the polypeptides of the protein map of Saccharomyces cerevisiae involved in glycolysis were investigated. This study resulted in a reassignment of two of the seven glycolytic enzyme polypeptides previously identified (Ludwig et al., Mol. Cell. Biol. 2:117-126, 1982), those corresponding to phosphoglycerate kinase and to alcohol dehydrogenase. It also resulted in the identification of two additional glycolytic polypeptides, the enolase B monomer and the glyceraldehyde phosphate dehydrogenase B monomer. The glycolytic enzymes polypeptides so identified were investigated in 5 laboratory strains (all S. cerevisiae) and in 11 commerical strains used for wine making (S. cerevisiae and Saccharomyces bayanus). It appeared highly significant that a particular electrophoretic variant of the glyceraldehyde phosphate dehydrogenase B monomer was found only in the wine yeasts. Furthermore, it was strongly suggested that S. cerevisiae and S. bayanus strains are distinguishible on the basis of a different electrophoretic migration of the enolase B monomer.
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PMID:Identification of Glycolytic Enzyme Polypeptides on the Two-Dimensional Protein Map of Saccharomyces cerevisiae and Application to the Study of Some Wine Yeasts. 1634 22