Microorganisms as Model Systems for Studying Evolution 1984
DOI: 10.1007/978-1-4684-4844-3_8
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Structural Evolution of Yeast Alcohol Dehydrogenase in the Laboratory

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Cited by 2 publications
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“…Within 400 generations, a mutant acid phosphatase with 60% greater activity at pH 6.0 and a pH optimum shifted to 4.8 was identified (a subsequent mutation caused clumping of the cells, reducing their likelihood of being washed out of the chemostat and illustrating that experimental evolution is somewhat like computer programming: you get exactly what you ask for, whether or not that was what you truly wanted). Selecting for mutant enzymes that discriminate between the natural substrate ethanol and the toxic analogue allyl alcohol63, 64 has altered the substrate specificity of alcohol dehydrogenase.…”
Section: Selection and Adaptationmentioning
confidence: 99%
“…Within 400 generations, a mutant acid phosphatase with 60% greater activity at pH 6.0 and a pH optimum shifted to 4.8 was identified (a subsequent mutation caused clumping of the cells, reducing their likelihood of being washed out of the chemostat and illustrating that experimental evolution is somewhat like computer programming: you get exactly what you ask for, whether or not that was what you truly wanted). Selecting for mutant enzymes that discriminate between the natural substrate ethanol and the toxic analogue allyl alcohol63, 64 has altered the substrate specificity of alcohol dehydrogenase.…”
Section: Selection and Adaptationmentioning
confidence: 99%