Hydrophobic binding is not an independent stereochemical determinant in the yeast glyoxalase I reaction

This publication has 17 references indexed in Scilit:

• Thiohemiacetal formation by inhibitory aldehydes at the active site of papain
  Biochemistry, 1977
• Glyoxalase I enzyme studies. 2. Nuclear magnetic resonance evidence for an enediol-proton transfer mechanism
  Journal of the American Chemical Society, 1976
• Effect of pH and thiols on the kinetics of yeast glyoxalase I. Evaluation of the random pathway mechanism
  Biochemistry, 1975
• Interpretations of enzyme reaction stereospecificity
  Accounts of Chemical Research, 1975
• Deuterium isotope effects and chemically modified coenzymes as mechanism probes of yeast glyoxalase-I
  Biochemistry, 1973
• The sterochemical configuration of the lactoyl group of S-lactoylglutathionine formed by the action of glyoxalase I from porcine erythrocytes and yeast
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1973
• Kinetic evaluation of substrate specificity in the glyoxalase-I-catalyzed disproportionation of α-ketoaldehydes
  Biochemistry, 1972
• A rapid assay for the glyoxalase enzyme system
  Analytical Biochemistry, 1971
• Organic Sulfur Compounds. XIII.¹ Free-Radical Addition of Thiols to Phenylacetylene²
  Journal of the American Chemical Society, 1964
• The effects of some analogues of glutathione on the glyoxalase system
  Biochemical Journal, 1957