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Related Experiment Videos

A Boudet1

  • 1Enzymologie et Métabolisme, Equipe de recherche Associée au C.N.R.S., Centre de Physiologie Végétale Université Paul Sabatier, 118, Route de Narbonne, 31, Toulouse, France

FEBS Letters
|May 10, 1971
PubMed
Summary
This summary is machine-generated.

Enzymes 5-dehydroquinate hydro-lyase and shikimate: NADP oxydoreductase in Quercus pedunculata roots appear to be associated. This enzyme aggregate has a molecular weight of approximately 55,000, similar to findings in Neurospora crassa.

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Area of Science:

  • Biochemistry
  • Plant Physiology
  • Enzymology

Background:

  • The shikimate pathway is crucial for plant secondary metabolism.
  • Understanding enzyme aggregation in plants can reveal metabolic regulation.
  • Quercus pedunculata is a significant tree species with potential biochemical relevance.

Purpose of the Study:

  • To investigate the potential association of 5-dehydroquinate hydro-lyase and shikimate: NADP oxydoreductase in Quercus pedunculata root extracts.
  • To determine the molecular weight of any associated enzyme complex.

Main Methods:

  • Enzyme activity assays for 5-dehydroquinate hydro-lyase and shikimate: NADP oxydoreductase.
  • Chromatographic separation techniques including Sephadex G 100, DEAE cellulose, and hydroxylapatite.

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  • Sucrose density gradient centrifugation.
  • Disc electrophoresis.
  • Gel filtration for molecular weight determination.

    • Main Results:

    • Both 5-dehydroquinate hydro-lyase and shikimate: NADP oxydoreductase activities consistently eluted together across multiple separation methods.
    • The observed co-elution suggests a stable association between these two enzymes.
    • Gel filtration indicated a molecular weight of approximately 55,000 for the enzyme aggregate.
    • The results are comparable to those found for the shikimate pathway enzyme aggregate in Neurospora crassa.

    Conclusions:

    • The findings strongly suggest that 5-dehydroquinate hydro-lyase and shikimate: NADP oxydoreductase exist as an associated complex in Quercus pedunculata root extracts.
    • This enzyme association may represent a functional or regulatory unit within the shikimate pathway in this plant species.
    • The conserved nature of this enzyme aggregation, as evidenced by comparison with Neurospora crassa, warrants further investigation into its biological significance.