Glucose 6-phosphate dehydrogenase from Saccharomyces cerevisiae: characterization of a reactive lysine residue labeled with acid

Abstract

Glucose-6-phosphate dehydrogenase from S. cerevisiae (bakers'' yeast) reacts with acteylsalicylcic acid, and this is accompanied by inactivation and modification of essentially 21 lysine residue/subunit. The amino acid sequence of an 11-residue tryptic peptide containing the reactive lysine residue of the yeast enzyme is given and establishes the existence of different subgroups of glucose-6-phosphate dehydrogenases. Thus, the labeled yeast structure has few similarities to the known structure around the reactive lysine residue of the enyzme from Leuconostoc mesenteroides, although it has extensive similarities with a structure in the human enyzme. It is further shown that amino acid sequences around reactive lysine residues of dehydrogenases in general vary, even though similarities occur around reactive lysine residues in 6-phosphogluconate, glutamate and glyceraldehyde-3-phosphate dehydrogenases.