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Selenocysteine

T C Stadtman1

  • 1National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.

Annual Review of Biochemistry
|January 1, 1996
PubMed
Summary
This summary is machine-generated.

Selenocysteine, the 21st amino acid, is incorporated via a unique UGA codon mechanism. Replacing cysteine with selenocysteine in enzymes can significantly alter or abolish their catalytic activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Selenocysteine is the 21st amino acid, incorporated during protein synthesis via the UGA codon.
  • This process involves unique tRNAs, a special elongation factor, and mRNA recognition elements.
  • Selenophosphate, a reactive selenium donor, is synthesized by selenophosphate synthetase found across diverse life forms.

Purpose of the Study:

  • To review the mechanisms of selenocysteine incorporation into proteins.
  • To discuss the distribution and properties of known selenocysteine-containing enzymes.
  • To explore the functional impact of selenocysteine in various enzyme families.

Main Methods:

  • Review of literature on selenocysteine biosynthesis and incorporation.
  • Analysis of known selenocysteine-containing enzymes and their properties.

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  • Discussion of studies involving artificial selenoenzymes and genetic engineering approaches.

    • Main Results:

    • Selenocysteine incorporation is a complex, ribosome-mediated process requiring specific factors and mRNA signals.
    • Selenocysteine is found in diverse enzymes, including glutathione peroxidases, deiodinases, and dehydrogenases.
    • Replacing selenocysteine with cysteine can drastically reduce or eliminate enzyme activity, as seen in glycine reductase.

    Conclusions:

    • Selenocysteine plays critical mechanistic roles in various enzymes, often essential for their catalytic function.
    • Understanding selenocysteine's role is vital for comprehending enzyme mechanisms and potential therapeutic applications.
    • Genetic engineering and chemical modification offer avenues for studying and creating novel selenoenzymes.