Saccharomyces cerevisiae phosphoglucose isomerase and fructose bisphosphate aldolase can be replaced functionally by the corresponding enzymes of Escherichia coli and Drosophila melanogaster.
Two glycolytic enzymes, phosphoglucose isomerase and fructose-1,6-bisphosphate aldolase, of Saccharomyces cerevisiae could be replaced by their heterologous counterparts from Escherichia coli and Drosophila melanogaster. Both heterologous enzymes, which show respectively little and no sequence homology to the corresponding yeast enzymes, fully restored wild-type properties when their genes were expressed in yeast deletion mutants. This result does not support notions of an obligatory formation of glycolytic multi-enzyme aggregates in yeast; nor does it support possible regulatory functions of yeast phosphoglucose isomerase.
Boles
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Institut für Mikrobiologie, Technische Hochschule Darmstadt, Federal Republic of Germany.
Zimmermann
F K
FK
D000818:Animals; D003001:Cloning, Molecular; D004331:Drosophila melanogaster / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000235:genetics*; D005816:Genetic Complementation Test; D005956:Glucose-6-Phosphate Isomerase / Q000235:genetics*; D006019:Glycolysis; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013045:Species Specificity
D009097:Multienzyme Complexes; D011994:Recombinant Proteins; D005634:Fructose-Bisphosphate Aldolase; D005956:Glucose-6-Phosphate Isomerase