Abstract
The fdp mutation has been localized on the genome of Saccharomyces carlsbergensis, on chromosome II, between lys2 and tyr1, at a man distance of 31 centimorgan from lys2. Since the fdp mutant does not grow on glucose, fructose, mannose and sucrose, hexose transport and a number of enzymes of carbon metabolism were tested, but no significant differences could be found between the wild type and the mutant. Only the regulatory properties of glycogen synthetase are changed in the mutant, but it is doubtful whether this can explain its phenotype. The disorganization of carbon metabolism of the mutant upon addition of glucose to the medium was analyzed in more detail. The most prominent feature observed until now is the accumulation of free glucose and hexose phosphates in the cell. This result indicates that somehow the feedback control between hexose transport and metabolism is impaired. Hexose phosphates are known to be toxic to many cells, including yeast. Therefore, accumulation of hexose phosphates in the presence of glucose in the medium, can explain the absence of growth on this carbon source.
MeSH Terms
Alcohol Oxidoreductases/metabolism
Fructose-Bisphosphatase/metabolism
Fructose-Bisphosphate Aldolase/metabolism
Genes, Regulator
Glucose/metabolism
Glucose-6-Phosphate Isomerase/metabolism
Glucosephosphate Dehydrogenase/metabolism
Hexokinase/metabolism
L-Lactate Dehydrogenase/metabolism
Mutation
Phosphofructokinase-1/metabolism
Phosphoglucomutase/metabolism
Phosphogluconate Dehydrogenase/metabolism
Pyruvate Decarboxylase/metabolism
Pyruvate Kinase/metabolism
Saccharomyces cerevisiae/enzymology
Chemicals
Alcohol Oxidoreductases
L-Lactate Dehydrogenase
Phosphogluconate Dehydrogenase
Glucosephosphate Dehydrogenase
Hexokinase
Phosphofructokinase-1
Pyruvate Kinase
Fructose-Bisphosphatase
Pyruvate Decarboxylase
Fructose-Bisphosphate Aldolase
Glucose-6-Phosphate Isomerase
Phosphoglucomutase
Glucose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
van de Poll K W
Schamhart D H
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16 references, click to expand
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