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S Liebe1, G Kopperschläger, W Diezel

  • 1Physiologisch-chemisches Institut der Karl-Marx-Universität, Leipzig, DDR

FEBS Letters
|May 11, 1970
PubMed
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Yeast phosphofructokinase (PFK) exhibits multiple active forms, from 180,000 to over 1 million daltons. Alkaline conditions fragment PFK into inactive subunits, revealing its complex polymeric structure.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Yeast phosphofructokinase (PFK) is a key glycolytic enzyme.
  • PFK activity is regulated by its molecular structure.
  • Understanding PFK's structure is crucial for metabolic studies.

Purpose of the Study:

  • To investigate the various molecular forms of yeast phosphofructokinase.
  • To elucidate the subunit composition and aggregation properties of PFK.
  • To propose a model for the structure-function relationship of PFK.

Main Methods:

  • Disc-electrophoresis was used to detect different molecular weight forms.
  • Analysis of enzyme fragmentation under alkaline conditions.
  • Molecular weight determination of active and inactive PFK species.

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Main Results:

  • Yeast PFK exists in multiple active forms (180,000–750,000 Da) and aggregates (>1 million Da).
  • Alkaline treatment yields inactive PFK fragments, suggesting a 60,000 Da subunit.
  • A model proposes active PFK as polymers of 180,000 Da monomers, each composed of three 60,000 Da subunits.

Conclusions:

  • Yeast PFK displays significant structural heterogeneity with distinct active forms.
  • The enzyme's structure is sensitive to pH, leading to fragmentation.
  • A subunit-based model explains the observed polymeric and aggregative states of PFK.