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Related Experiment Videos

Structure-function relationship of bromelain isoinhibitors from pineapple stem.

Ken-ichi Hatano1, Yoriko Sawano, Masaru Tanokura

  • 1Department of Biological Sciences, Faculty of Engineering, Gunma University, Kiryu, Japan.

Biological Chemistry
|November 20, 2002
PubMed
Summary

Bromelain isoinhibitors (BIs) from pineapple stems are unique double-chain cysteine proteinase inhibitors. Unexpectedly, their structure resembles Bowman-Birk inhibitors (BBI), suggesting a shared evolutionary origin and functional divergence.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Evolution

Background:

  • Bromelain isoinhibitors (BIs) are double-chain inhibitors found in pineapple stems.
  • They function by competitively inhibiting the cysteine proteinase bromelain.

Purpose of the Study:

  • To elucidate the three-dimensional structure of BIs.
  • To compare the structural features of BIs with known proteinase inhibitor families.

Main Methods:

  • X-ray crystallography or NMR spectroscopy to determine the 3D structure of BIs.
  • Comparative structural analysis with databases of protein structures.

Main Results:

  • BIs possess a unique double-domain structure, each domain featuring a three-stranded anti-parallel beta-sheet.

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  • BIs exhibit structural and disulfide-bond connectivity similarities to Bowman-Birk trypsin/chymotrypsin inhibitor (BBI).
  • No structural similarity was found with the cystatin superfamily.

    • Conclusions:

    • The structural similarity between BIs and BBI suggests a common evolutionary ancestor.
    • BIs and BBI likely diverged in function over evolutionary time.
    • This finding provides insights into the evolution of proteinase inhibitors.