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Related Experiment Videos

Yeast 6-phosphofructo-2-kinase: sequence and mutant.

M Kretschmer1, D G Fraenkel

  • 1Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.

Biochemistry
|November 5, 1991
PubMed
Summary
This summary is machine-generated.

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Yeast 6-phosphofructo-2-kinase (PFK26) has a distinct structure compared to its rat liver counterpart, lacking bisphosphatase activity. A second enzyme contributes to fructose-2,6-bisphosphate levels in yeast.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Metabolism

Background:

  • Yeast 6-phosphofructo-2-kinase (PFK26) is a key enzyme in glycolysis.
  • Its structural and functional relationship to mammalian bifunctional enzymes was previously unclear.
  • The regulation of fructose-2,6-bisphosphate (F2,6P2) levels in yeast is complex.

Purpose of the Study:

  • To characterize the yeast PFK26 gene and protein.
  • To elucidate the structural and functional differences between yeast PFK26 and rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
  • To identify other enzymes involved in yeast F2,6P2 synthesis.

Main Methods:

  • Gene sequencing of yeast PFK26.
  • Amino acid sequence analysis and comparison with homologous enzymes.

Related Experiment Videos

  • Construction and analysis of a yeast chromosomal null mutant (pfk26::LEU2).
  • Enzyme activity assays and affinity chromatography.

    • Main Results:

    • Yeast PFK26 has an 827-amino acid, 93.5-kDa subunit with 42% identity to rat liver enzyme.
    • Key differences include a serine instead of histidine at a critical active site residue, explaining the lack of bisphosphatase activity.
    • The yeast enzyme has a putative C-terminal phosphorylation site for activation and lacks the N-terminal inhibitory site of the liver enzyme.
    • A pfk26 mutant showed marginal activity but grew normally on glucose, maintaining near-normal F2,6P2 levels.
    • The mutant's F2,6P2 levels were undetectable during growth on pyruvate and did not increase upon glucose addition with cycloheximide.
    • A second, glucose-inducible enzyme was identified, contributing to F2,6P2 synthesis, particularly in the absence of PFK26.

    Conclusions:

    • Yeast PFK26 is a dedicated 6-phosphofructo-2-kinase lacking bisphosphatase activity.
    • Its regulatory properties differ significantly from the mammalian bifunctional enzyme.
    • A second enzyme plays a crucial role in yeast fructose-2,6-bisphosphate metabolism, especially under specific growth conditions.