Effects of substrate structure and temperature on the stereospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus

This publication has 15 references indexed in Scilit:

• Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.
  Published by Elsevier ,2021
• Different enzymic reactions of an enantiomeric pair: simultaneous dual kinetic resolution of a keto ester by bakers' yeast
  The Journal of Organic Chemistry, 1987
• Thermostable enzymes in organic synthesis. 2. Asymmetric reduction of ketones with alcohol dehydrogenase from Thermoanaerobium brockii
  Journal of the American Chemical Society, 1986
• Enzyme catalysed hydrolysis of dialkylated propanedioic acid diesters, chain length dependent reversal of enantioselectivity
  Tetrahedron, 1985
• Microbial Asymmetric Catalysis—Enantioselective Reduction of Ketones [New Synthetic Methods (45)]
  Angewandte Chemie International Edition in English, 1984
• Mechanistic deductions from isotope effects in multireactant enzyme mechanisms
  Biochemistry, 1981
• Enzymes in organic synthesis. 14. Stereoselective horse liver alcohol dehydrogenase catalyzed oxidations of diols containing a prochiral centre and of related hemiacetals
  Canadian Journal of Chemistry, 1979
• Asymmetric syntheses via enantiotopically selective horse liver alcohol dehydrogenase catalyzed oxidations of diols containing a prochiral center
  Journal of the American Chemical Society, 1977
• A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
  Analytical Biochemistry, 1976
• Substrate Specificity and Stereospecificity of Alcohol Dehydrogenases
  Nature, 1967