Novel cofactors via post-translational modifications of enzyme active sites

Chem Biol. 2000 Jul;7(7):R159-71. doi: 10.1016/s1074-5521(00)00140-x.

Abstract

Recent crystallographic and biochemical studies have revealed the existence of numerous novel post-translational modifications within enzyme active sites. These modifications create structural and functional diversity. Although the function and biosynthesis of some of these modifications are well understood, others need further investigation.

Publication types

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

MeSH terms

  • Animals
  • Binding Sites
  • Catalytic Domain / physiology*
  • Coenzymes / metabolism*
  • Enzymes / chemistry*
  • Enzymes / metabolism*
  • Humans
  • Metalloproteins
  • Models, Molecular
  • Molecular Structure
  • Protein Conformation
  • Protein Processing, Post-Translational / physiology*
  • Tyrosine / chemistry

Substances

  • Coenzymes
  • Enzymes
  • Metalloproteins
  • Tyrosine