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Zinc enzymes

J E Coleman1

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, PO Box 208114, New Haven, CT 06520-8114, USA. coleman@zinc.csb.yale.edu

Current Opinion in Chemical Biology
|July 17, 1998
PubMed
Summary
This summary is machine-generated.

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Zinc enzymes, crucial for biological processes, primarily catalyze hydrolysis and transfer reactions. Their structural and mechanistic data reveal how Zn2+ activates water molecules for nucleophilic attack on substrates.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • The availability of detailed structural and mechanistic data for zinc enzymes is rapidly increasing.
  • Zinc enzymes play vital roles in numerous biological pathways.

Purpose of the Study:

  • To summarize the current understanding of zinc enzyme catalysis based on emerging structural and mechanistic data.
  • To highlight the catalytic mechanisms employed by zinc enzymes, particularly their interaction with substrates.

Main Methods:

  • Analysis of high-resolution crystal structures of zinc enzymes.
  • Review of mechanistic studies on zinc enzyme-catalyzed reactions.
  • Integration of structural and kinetic data to elucidate catalytic mechanisms.

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Main Results:

  • The majority of characterized zinc enzymes catalyze hydrolysis or closely related transfer reactions.
  • Tetrahedral or 5-coordinate Zn2+ in a protein environment effectively activates water as a nucleophile.
  • Zn2+ facilitates catalysis by forming mixed complexes with substrates, altering coordination, or exchanging ligands.

Conclusions:

  • Protein-bound Zn2+ is ideally suited for activating nucleophiles and polarizing substrates.
  • The catalytic mechanisms involve precise positioning and electronic manipulation of substrates by Zn2+.
  • Emerging data reinforce the central role of zinc in enzyme-catalyzed hydrolysis and transfer reactions.