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Catalytic triads and their relatives

G Dodson1, A Wlodawer

  • 1Dept of Chemistry, University of York, UK.

Trends in Biochemical Sciences
|October 27, 1998
PubMed
Summary
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Enzymes use a catalytic triad of Asp-His-Ser residues to activate serine nucleophiles for substrate hydrolysis. This catalytic triad pattern is conserved across many hydrolytic enzymes, demonstrating protein adaptability.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • The serine protease catalytic triad (Asp-His-Ser) is crucial for enzyme activity.
  • This triad's specific arrangement within the enzyme-substrate complex activates the seryl hydroxyl group for nucleophilic attack.
  • Subtilisin and trypsin families exhibit highly conserved catalytic triad compositions and arrangements.

Purpose of the Study:

  • To review the conservation and variation of catalytic triad residues in hydrolytic enzymes.
  • To understand how proteins adapt to generate catalytic stereochemistry on diverse frameworks.
  • To explore the mechanisms of nucleophilic attack by serine or threonine residues in various enzymes.

Main Methods:

  • Comparative analysis of catalytic triad residue patterns across different hydrolytic enzymes.

Related Experiment Videos

  • Literature review focusing on enzyme mechanisms and protein structural variations.
  • Examination of sequence and organizational differences in catalytic residues.

    • Main Results:

    • While the Asp-His-Ser pattern is conserved in some proteases, other hydrolytic enzymes utilize variations.
    • The acid-base-serine/threonine pattern is generally conserved, but specific acidic and basic residues can differ.
    • Observed variations highlight protein adaptability in creating catalytic sites for diverse substrates.

    Conclusions:

    • The catalytic triad's fundamental role in activating nucleophilic residues is broadly conserved in hydrolytic enzymes.
    • Enzyme evolution demonstrates significant flexibility in the specific composition and arrangement of catalytic residues.
    • These variations allow proteins to achieve specific catalytic functions and stereochemistry across a wide range of substrates.