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The alpha/beta hydrolase fold.

D L Ollis1, E Cheah, M Cygler

  • 1Research School of Chemistry, Australian National University, Canberra.

Protein Engineering
|April 1, 1992
PubMed
Summary
This summary is machine-generated.

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Researchers discovered a common alpha/beta hydrolase fold in diverse enzymes. This protein fold preserves catalytic triad arrangements, revealing evolutionary convergence in enzyme active sites.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Hydrolytic enzymes exhibit diverse phylogenetic origins and functions.
  • A common structural motif, the alpha/beta hydrolase fold, has been identified across these enzymes.

Purpose of the Study:

  • To identify and characterize a novel protein fold common to various hydrolytic enzymes.
  • To investigate the evolutionary relationships and conserved features of these enzymes.

Main Methods:

  • Structural analysis of multiple hydrolytic enzymes.
  • Sequence comparison to identify conserved elements.

Main Results:

  • Identification of the alpha/beta hydrolase fold, characterized by an eight-stranded beta-sheet core flanked by alpha-helices.

Related Experiment Videos

  • Conservation of catalytic triad residues (nucleophile-histidine-acid) on structurally conserved loops.
  • The arrangement of catalytic residues is conserved, not the binding site, suggesting divergence from a common ancestor.
  • The catalytic triad arrangement is a mirror image of that found in serine proteases.

    • Conclusions:

    • The alpha/beta hydrolase fold represents a conserved structural framework enabling convergent evolution of enzyme active sites.
    • Four enzyme groups, including eukaryotic serine proteases, cysteine proteases, subtilisins, and alpha/beta hydrolase fold enzymes, utilize catalytic triads evolved convergently.
    • Structural conservation of catalytic triad loops highlights their importance in maintaining enzyme function across diverse evolutionary paths.