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Related Experiment Videos

Covalent cofactor binding to flavoenzymes requires specific effectors.

R Brandsch1, V Bichler

  • 1Biochemisches Institut, Universität Freiburg, Federal Republic of Germany.

European Journal of Biochemistry
|June 1, 1989
PubMed
Summary
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Metabolic intermediates like glyceraldehyde-3-phosphate and citrate activate flavoenzymes, such as 6-hydroxy-D-nicotine oxidase and fumarate reductase, by promoting covalent FAD attachment. This covalent modification is crucial for enzyme activity and suggests allosteric regulation.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Covalent flavinylation, involving FAD attachment to histidine residues, is a known modification in several flavoenzymes.
  • Examples include 6-hydroxy-D-nicotine oxidase (6-HDNO) and flavoprotein subunits of fumarate reductase and succinate dehydrogenase.

Purpose of the Study:

  • To investigate the role of specific metabolic intermediates in the formation of active holoenzymes from their apoforms.
  • To explore the influence of glycolytic and citric acid cycle intermediates on flavoenzyme activation.

Main Methods:

  • Monitoring holoenzyme formation via [14C]FAD incorporation and enzyme activity assays.
  • Utilizing a riboflavin-requiring E. coli strain overexpressing specific operons for apoflavoprotein production.

Related Experiment Videos

  • Analyzing flavinylation through polyacrylamide gel electrophoresis and fluorography.

    • Main Results:

    • Phosphoenolpyruvate, glyceraldehyde-3-P, glycerate-3-P, and glycerol-3-P were found to mediate 6-HDNO holoenzyme formation.
    • Citrate, isocitrate, succinate, and fumarate significantly stimulated flavinylation of fumarate reductase and succinate dehydrogenase apoflavoproteins.
    • Enzyme activation correlated with covalent FAD incorporation.

    Conclusions:

    • Specific metabolic intermediates are essential for the covalent modification and activation of flavoenzymes.
    • These intermediates may function as allosteric effectors regulating enzyme activity.
    • This highlights a metabolic link to flavoenzyme function and regulation.