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To what extent do structural changes in catalytic metal sites affect enzyme function?

Yana Valasatava1, Antonio Rosato1, Nicholas Furnham2

  • 1Magnetic Resonance Center, University of Florence, 50019 Sesto Fiorentino, Italy; Department of Chemistry, University of Florence, 50019 Sesto Fiorentino, Italy.

Journal of Inorganic Biochemistry
|November 22, 2017
PubMed
Summary
This summary is machine-generated.

Metalloenzyme superfamilies show conserved metal sites, with non-redox metals maintaining their catalytic roles despite structural changes. Redox-active metals, however, often change catalytic roles when metal sites evolve.

Keywords:
Bioinorganic chemistryCopperEnzymesEvolutionIronMagnesiumMetallo-proteinsZinc

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Area of Science:

  • Biochemistry
  • Enzymology
  • Evolutionary Biology

Background:

  • Metals are crucial cofactors in approximately half of all known enzymatic reactions.
  • Enzyme superfamilies often exhibit functional diversification while retaining a conserved structural scaffold.
  • Understanding the interplay between structural changes and functional evolution in metalloenzymes is key.

Purpose of the Study:

  • To investigate the relationship between functional differentiation and structural alterations at the catalytic metal site within metalloenzyme superfamilies.
  • To determine how evolutionary changes in metal-binding sites impact enzyme function and catalytic mechanisms.

Main Methods:

  • Comparative analysis of metalloenzyme superfamilies.
  • Examination of structural variations within catalytic metal sites.
  • Correlation of structural changes with functional diversification and catalytic roles.

Main Results:

  • Metalloenzyme superfamilies generally conserve their catalytic metal sites during evolution.
  • When metal sites remain unchanged, functional differentiation is typically low and mechanisms are conserved.
  • High functional differentiation correlates with diverse structural changes in the metal-binding site.
  • Non-redox metal roles are highly conserved, even with significant structural modifications.
  • Redox-active metal roles are altered in over 50% of cases with metal site changes.
  • Metal sites with redox roles are never lost during evolution within the studied dataset.

Conclusions:

  • The catalytic role of metal ions is a highly conserved feature in metalloenzyme evolution.
  • Functional diversification in metalloenzymes is often driven by changes in the surrounding protein matrix, especially for non-redox metals.
  • Evolutionary modifications at the metal site significantly impact the catalytic role of redox-active metals.