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Related Experiment Videos

Proteolytic activities in yeast.

T Saheki, H Holzer

    Biochimica Et Biophysica Acta
    |March 28, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Yeast proteinase activation occurs through the breakdown of inhibitors, not zymogen activation. Proteinase A plays a key role in activating proteinases B and C by degrading their inhibitors.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Yeast Molecular Biology

    Background:

    • Yeast proteinases A, B, and C are crucial enzymes.
    • Their activation mechanisms in crude yeast extracts were previously unclear.

    Purpose of the Study:

    • To elucidate the mechanism and time course of yeast proteinase A, B, and C activation.
    • To investigate the role of proteinase A and inhibitors in this process.

    Main Methods:

    • Crude yeast extracts were incubated at pH 5.1 and 25°C.
    • Proteinase activities and inhibitor levels were monitored over time.
    • The effects of purified proteinase A and pepstatin were examined.

    Main Results:

    • Proteinase B activity increase correlated with proteinase B inhibitor disappearance.

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  • Proteinase A accelerated inhibitor inactivation and proteinase B and C activation.
  • Pepstatin inhibited proteinase A, retarding inhibitor degradation and proteinase B activation.
  • Yeast grown on complete medium showed slower activation compared to minimal medium.

    • Conclusions:

    • Yeast proteinase activation results from proteolytic digestion of inhibitors, not zymogen activation.
    • Proteinase A is essential for the activation cascade by degrading inhibitors.
    • Growth conditions influence the rate of proteinase activation due to varying inhibitor levels.