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Applied and Environmental Microbiology, April 2001, p. 1587-1593, Vol. 67, No. 4
Faculty of Science, Swammerdam Institute for
Life Science, University of Amsterdam, 1018 TV
Amsterdam,1 and Faculty of Biology,
Department of Molecular Cell Physiology, Free University, 1081 HV
Amsterdam,2 The Netherlands
Received 22 September 2000/Accepted 29 December 2000
Hexokinase II is an enzyme central to glucose metabolism and
glucose repression in the yeast Saccharomyces cerevisiae.
Deletion of HXK2, the gene which encodes hexokinase
II, dramatically changed the physiology of S. cerevisiae. The hxk2-null mutant strain displayed fully oxidative growth at high glucose concentrations in early exponential batch cultures, resulting in an initial absence of fermentative products such as ethanol, a postponed and shortened diauxic shift, and higher biomass yields. Several intracellular changes
were associated with the deletion of hexokinase II. The hxk2 mutant had a higher mitochondrial
H+-ATPase activity and a lower pyruvate decarboxylase
activity, which coincided with an intracellular accumulation of
pyruvate 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
mutant than in the wild type. The results suggest a redirection of
carbon flux in the hxk2 mutant to the production of biomass
as a consequence of reduced glucose repression.
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.4.1587-1593.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Physiological Properties of Saccharomyces
cerevisiae from Which Hexokinase II Has Been Deleted
*
Corresponding author. Mailing address: Instituut voor
Interdisciplinaire Opleidingen (I2O), Sarphatistraat 104, 1018 GV Amsterdam, The Netherlands. Phone: 31 (20) 525 5510. Fax: 31 (20) 525 5505. E-mail: k.van.dam{at}chem.uva.nl.
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