Influence of the oligomeric state of yeast hexokinase isozymes on inactivation and unfolding by urea.

The effect of the association-dissociation equilibrium on the urea-induced inactivation and unfolding of the yeast hexokinase isoforms, PI and PII, showed that these enzymes are more stable as dimers. For the monomeric PII, the inactivation and unfolding processes occurred in parallel. However, inactivation precedes the unfolding of monomeric PI or dimeric PI and PII. The unfolding transitions are biphasic for PI indicating stable intermediates, whereas for the PII isoform the unfolding occurs in a single step. Our data suggests that although PI and PII present a 78% identity in their amino acid sequences, they probably have distinct inactivation and unfolding by urea behavior.