Posttranslational Modification of Proteins by Christopher Walsh - First Edition, 2006 from Macmillan Student Store
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Posttranslational Modification of Proteins

First  Edition©2006 Christopher Walsh

About

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.

Table of Contents

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

Christopher Walsh

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 elucidated the catalytic mechanisms of a wide variety of enzymes including flavoproteins and other redox enzymes. He has also pioneered the design of mechanism-based enzyme inhibitors (or "suicide" substrates). His work has found practical application in the design of antibacterial agents, anticonvulsive agents, plant growth regulators, and antitumor drugs. His current focus is on the biosynthesis and mechanism of action of antibiotics and bacterial siderophores. He has published over 600 scientific articles and his book, Enzymatic Reaction Mechanisms, has educated generations of enzymologists.

Professor Walsh's accomplishments have been recognized through numerous awards which include the Eli Lilly Award in Biochemistry, the Arthur C. Cope Scholar Award in Organic Chemistry, the Repligen Award in Biological Chemistry, and the Alfred Bader Award in Bioorganic and Bioinorganic Chemistry. He is a member of the National Academy of Sciences, the Institute of Medicine, and the American Academy of Arts and Sciences.