Ja. Diderich et al., Physiological properties of Saccharomyces cerevisiae from which hexokinaseII has been deleted, APPL ENVIR, 67(4), 2001, pp. 1587-1593
Hexokinase II is an enzyme central to glucose metabolism and glucose repres
sion in the yeast Saccharomyces cerevisiae. Deletion of HXK2, the gene whic
h encodes hexokinase II, dramatically changed the physiology of S. cerevisi
ae. The hxk2-null mutant strain displayed fully oxidative growth at high gl
ucose concentrations in early exponential batch cultures, resulting in an i
nitial absence of fermentative products such as ethanol, a postponed and sh
ortened diauxic shift, and higher biomass yields. Several intracellular cha
nges were associated with the deletion of hexokinase II. The hxk2 mutant ha
d a higher mitochondrial H+-ATPase activity and a lower pyruvate decarboxyl
ase activity, which coincided with an intracellular accumulation of pyruvat
e in the hxk2 mutant. The concentrations of adenine nucleotides, glucose-6-
phosphate, and fructose-6-phosphate are comparable in the wild type and the
hxk2 mutant. In contrast, the concentration of fructose-1,6-bisphosphate,
an allosteric activator of pyruvate kinase, is clearly lower in the hxk2 mu
tant than in the wild type. The results suggest a redirection of carbon flu
x in the hxk2 mutant to the production of biomass as a consequence of reduc
ed glucose repression.