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Posttranslational Modification of Proteins
Christopher T Walsh
Harvard Medical School
500 pages
Publisher:
Roberts & Company, USA
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.
Posttranslational Modification of Proteins is the first comprehensive treatment of this burgeoning area of proteome diversification.
Preface
Introduction
Phosphorylation and dephosphorylation
Sulfurylation of proteins
Sulfur redox transformations in proteins
Protein methylation
Protein acetylation
Lipid modifications of proteins
Posttranslational proteolysis
Ubiquitin and ubiquitin like protein tags
Protein glycosylation
ADP ribosylation of proteins
Protein hydroxylation
Automodification reactions of proteins
Swinging arms for covalent tethering of coenzymes
Protein carboxyaltion and amidation
References
Index
Christopher 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. 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.
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