Yeast glyoxalase I. Circular dichroic spectra and pH effects.
Large scale isolation and physicochemical characterisation of yeast glyoxalase I showed that this enzyme contained small amounts of carbohydrates. Circular dichroic spectra of the enzyme measured in the presence and absence of S-(p-bromobenzyl)glutathione indicated perturbation of a tyrosine on binding of this competitive inhibitor. Values of Ki for competitive inhibitors were pH invariant over the accessible pH range.
D002241:Carbohydrates / Q000032:analysis; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007791:Lactoylglutathione Lyase / Q000302:isolation & purification / Q000378:metabolism*; D008190:Lyases / Q000378:metabolism*; D008970:Molecular Weight; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D002241:Carbohydrates; D008190:Lyases; D007791:Lactoylglutathione Lyase