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Catalysis by Yeast Alcohol Dehydrogenase

  • Bryce V. Plapp
  • Axel J. Ganzhorn
  • Robert M. Gould
  • David W. Green
  • Tobias Jacobi
  • Edda Warth
  • Darla Ann Kratzer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)

Abstract

The structure and mechanism of alcohol dehydrogenases have been extensively studied (Bränden et al., 1975; Klinman, 1981; Pettersson, 1987). The three-dimensional structures of the horse liver enzyme in several ternary complexes have been solved at high resolution (Eklund et al., 1981, 1982). Amino acid sequences for more than 22 NAD+-dependent alcohol dehydrogenases from 11 animal, plant and fungal species are known. Comparison of these sequences raises many questions about the structure-function relationships in these enzymes. How do the amino acid residues at the active site participate in catalysis? What is the basis of substrate specificity? What was selected for during the evolution of the different enzymes?

Keywords

Alcohol Dehydrogenase Wild Type Enzyme Mutant Enzyme Substrate Binding Pocket Horse Liver 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Bryce V. Plapp
    • 1
  • Axel J. Ganzhorn
    • 1
  • Robert M. Gould
    • 1
  • David W. Green
    • 1
  • Tobias Jacobi
    • 1
  • Edda Warth
    • 1
  • Darla Ann Kratzer
    • 1
  1. 1.Department of BiochemistryThe University of IowaIowa CityUSA

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