Is the phosphofructokinase‐reaction obligatory for glucose fermentation by <i>Saccharomyces cerevisiae</i>?

Heinisch, Jürgen; Zimmerman, Friedrich K.

doi:10.1002/yea.320010205

Cited by 13 publications

(3 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since mutants lacking one of the two phosphofructokinase genes ferment glucose but do not show phosphofructokinase activity in vitro, a pathway bypassing this reaction was proposed. This bypass should include reactions of the nonoxidative part of the pentosephosphate pathway [12].…”

Section: Molecular Analysis Of the Structural Gene For Yeast Transaldmentioning

confidence: 99%

Molecular analysis of the structural gene for yeast transaldolase

Schaaff

Hohmann

Zimmermann

1990

European Journal of Biochemistry

View full text Add to dashboard Cite

We have cloned the structural gene for yeast transaldolase. Transformants carrying the TALl gene on a multicopy plasmid over-produced transaldolase. A deletion mutant which was constructed using the cloned gene did not show any detectable transaldolase activity in vitro. Furthermore, both transaldolase isoenzymes which were detected in wild-type crude extracts by immunoblotting were missing in the deletion mutants. Thus, TALl is the only transaldolase structural gene in yeast.TALI is not an essential gene. Deletion of the transaldolase gene did not affect growth on complete media with different carbon sources or on synthetic media. However, the transaldolase-deficient strains accumulated sedoheptulose 7-phosphate, an intermediate of the pentose-phosphate pathway. Mutants lacking both transaldolase and phosphoglucose isomerase grew more slowly than the single mutants. They accumulated more sedoheptulose 7-phosphate on medium containing fructose than on glucose medium. This shows that fructose 6-phosphate and glyceraldehyde 3-phosphate, metabolites of glycolysis, can enter the nonoxidative part of the pentose-phosphate pathway.

show abstract

Section: Molecular Analysis Of the Structural Gene For Yeast Transaldmentioning

confidence: 99%

Molecular analysis of the structural gene for yeast transaldolase

Schaaff

Hohmann

Zimmermann

1990

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…With the advance of powerful tools in yeast genetics, the models obtained from formal biochemistry have been at large substantiated by mutant studies, as well as the results gathered by molecular genetic techniques (reviewed by Wills, 1990; and by Heinisch and Hollenberg, 1993). Thus, in general, deletion mutants in glycolytic genes leading to a complete loss of in vitro detectable enzymatic activity displayed a deficiency for growth on media containing glucose, with the exception of those encoding the subunits of yeast phosphofructokinase (Heinisch and Zimmermann, 1985). The latter mutants could grow on glucose, a phenotype which has been attributed to an in vivo Pfk activity of the remaining subunits that is undetectable by in vitro assays (Arvanitidis and Heinisch, 1994).…”

Section: Introductionmentioning

confidence: 99%

Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase

Heinisch

Müller

Schlüter

et al. 1998

Yeast

View full text Add to dashboard Cite

Our previous data indicated that GPM1 encodes the only functional phosphoglycerate mutase in yeast. However, in the course of the yeast genome sequencing project, two homologous sequences, designated GPM2 and GPM3, were detected. They have been further investigated in this work. Key residues in the deduced amino acid sequence, shown to be involved in catalysis for Gpm1 (i.e. His8, Arg59, His181) are conserved in both enzymes. Overexpression of the genes under control of their own promoters in a gpm1 deletion mutant did not complement for any of the phenotypes. This could in part be attributed to a lack of expression due to their weak promoters. Higher level expression under the control of the yeast PFK2 promoter partially complemented the gpm1 defects, without restoring detectable enzymatic activity. Nevertheless, deletion of either GPM2 or GPM3, or the two deletions in concert, did not produce any obvious lesions for growth on a variety of different carbon sources, nor did they change the levels of key intermediary metabolites. We conclude that both genes evolved from duplication events and that they probably constitute non‐functional homologues in yeast.

show abstract

“…interpreted as each subunit still having catalytic activity undetectable by in vitro assays, or by the involvement of the subunits in a separate pathway of glucose fermentation (HEINISCH and ZIMMERMANN, 1985). Further analysis to distinguish between these possibilities is in progress.…”

Section: 7140mentioning

confidence: 99%