The number of protein isoforms in proteomes can be two to three orders of magnitude higher than the number of genes in the genomes. This is in large part due to posttranslational modifications of proteins that provide covalent alterations to protein backbones and side chains that increase proteome complexities. Greater than 5% of the genes in the human genome encode enzymes that perform such modifications, including hundreds of protein kinases and opposing phosphatases, ubiquitinyl ligases, acetylases and deacetylases, methyl transferases and glycosyl transferases. The major classes of posttranslational modifications (PTM) are codified according to types of residues modified, underlying chemistry, PTM catalysts, and biological consequences. This is the first comprehensive treatment of this burgeoning area of proteome diversification. Contents: Preface; 1. Introduction; 2. Phosphorylation and dephosphorylation; 3. Sulfurylation of proteins; 4. Sulfur redox transformations in proteins; 5. Protein methylation; 6. Protein acetylation; 7. Lipid modifications of proteins; 8. Posttranslational proteolysis; 9. Ubiquitin and ubiquitin-like protein tags; 10. Protein glycosylation; 11. ADP ribosylation of proteins; 12. Protein hydroxylation; 13. Automodification reactions of proteins; 14. Swinging arms for covalent tethering of coenzymes; 15. Protein carboxyaltion and amidation; References; Index.
Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.
Professor Walsh is currently the Hamilton Kuhn Professor of Biological Chemistry and Molecular Pharmacology at Harvard Medical School. He is one of the leading enzymologists in the world. He has published over 600 scientific articles and his book, Enzymatic Reaction Mechanisms (WH Freeman), has educated generations of enzymologists.
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