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Related Experiment Videos

The dissociated tryptophanase subunit is inactive

O Raibaud, M E Goldberg

    The Journal of Biological Chemistry
    |May 10, 1976
    PubMed
    Summary
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    Apotryptophanase dissociation into dimers is governed by hydrophobic interactions, as indicated by the Hofmeister series. The enzyme

    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Dynamics

    Background:

    • Apotryptophanase exists as a tetramer, but can dissociate into dimers.
    • Understanding the equilibrium between dimer and tetramer forms is crucial for enzyme function.

    Purpose of the Study:

    • To investigate the interactions governing the dimer-tetramer equilibrium of apotryptophanase.
    • To determine the effect of dissociation on the enzyme's functional properties.

    Main Methods:

    • Studied the dimer-tetramer equilibrium using anions that follow the Hofmeister series.
    • Investigated the kinetics of active enzyme formation from dimeric apotryptophanase in the presence of cofactor and substrate.

    Main Results:

    • Anion-induced shifts in equilibrium align with the Hofmeister series, indicating hydrophobic interactions are key.

    Related Experiment Videos

  • Reassociation kinetics are second order in enzyme concentration and independent of pyridoxal-P.
  • The rate constant for reassociation was determined as 5 x 10^4 M^-1 S^-1.

    • Conclusions:

    • Hydrophobic interactions primarily drive the dimer-tetramer association of apotryptophanase.
    • The reassociation of dimers into tetramers is the rate-limiting step for enzymatic activity.
    • Dimeric apotryptophanase is functionally inactive.