Natural and synthetic selenoproteins

Curr Opin Chem Biol. 2014 Oct:22:27-34. doi: 10.1016/j.cbpa.2014.09.010. Epub 2014 Sep 28.

Abstract

Once considered highly toxic, the element selenium is now recognized as a micronutrient essential for human health. It is inserted co-translationally into many proteins as the non-canonical amino acid selenocysteine, providing the resulting selenoprotein molecules with a range of valuable redox properties; selenocysteine is also increasingly exploited as a structural and mechanistic probe in synthetic peptides and proteins. Here we review topical investigations into the preparation and characterization of natural and artificial selenoproteins. Such molecules are uniquely suited as tools for protein chemistry and as a test bed for studying novel catalytic activities.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Oxidation-Reduction
  • Protein Biosynthesis
  • Protein Folding
  • Recombinant Proteins / chemical synthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Selenocysteine / chemical synthesis
  • Selenocysteine / chemistry*
  • Selenocysteine / genetics
  • Selenocysteine / metabolism
  • Selenoproteins / chemical synthesis
  • Selenoproteins / chemistry*
  • Selenoproteins / genetics
  • Selenoproteins / metabolism

Substances

  • Recombinant Proteins
  • Selenoproteins
  • Selenocysteine