Evaluation of the two‐substrate pathway of glyoxalase I from yeast by use of carbonic anhydrase and rapid‐kinetic studies

This publication has 13 references indexed in Scilit:

• Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources
  Biochemical Journal, 1979
• Binding of the competitive inhibitor S -(p -bromobenzyl)-glutathione to glyoxalase I from yeast
  FEBS Letters, 1979
• Subunit structure of glyoxalase I from yeast
  FEBS Letters, 1978
• Effect of pH and thiols on the kinetics of yeast glyoxalase I. Evaluation of the random pathway mechanism
  Biochemistry, 1975
• Regulatory Behavior of Monomeric Enzymes
  European Journal of Biochemistry, 1974
• α-Keto Esters as Substrates of Erythrocyte Carbonic Anhydrase. Kinetic Studies of Enzyme Catalyzed Hydration of Methyl and Ethyl Pyruvate.
  Biochemistry, 1974
• The Steady‐State Kinetics of Glyoxalase I from Porcine Erythrocytes
  European Journal of 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
• Discrimination between steady-state kinetic models of the mechanism of action of yeast glyoxalase
  Biochemistry, 1973
• The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. I. Kinetic Studies of the Enzyme-Catalyzed Hydration of Acetaldehyde^*
  Biochemistry, 1965