Protein posttranslational modifications: The chemistry of proteome diversifications

Christopher T. Walsh, Sylvie Garneau-Tsodikova, Gregory J. Gatto

Research output: Contribution to journalReview articlepeer-review

1143 Scopus citations

Abstract

The diversity of distinct covalent forms of proteins (the proteome) greatly exceeds the number of proteins predicted by DNA coding capacities owing to directed posttranslational modifications. Enzymes dedicated to such protein modifications include 500 human protein kinases, 150 protein phosphatases, and 500 proteases. The major types of protein covalent modifications, such as phosphorylation, acetylation, glycosylation, methylation, and ubiquitylation, can be classified according to the type of amino acid side chain modified, the category of the modifying enzyme, and the extent of reversibility. Chemical events such as protein splicing, green fluorescent protein maturation, and proteasome autoactivations also represent posttranslational modifications. An understanding of the scope and pattern of the many posttranslational modifications in eukaryotic cells provides insight into the function and dynamics of proteome compositions.

Original languageEnglish
Pages (from-to)7342-7372
Number of pages31
JournalAngewandte Chemie - International Edition
Volume44
Issue number45
DOIs
StatePublished - Dec 1 2005

Keywords

  • Amino acids
  • Enzymes
  • Protein modifications
  • Proteomics

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

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