Posttranslational Modification of Proteins: Expanding Nature's Inventory / Edition 1

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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.

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Editorial Reviews

From the Publisher
"Christopher Walsh, an acclaimed scientist, has written yet another outstanding book. It surveys the vast field of chemical modifications that proteins undergo in living cells. The book's depth of coverage and clarity of exposition will make it an indispensable text for both students and active researchers."
—Alexander Varshavsky, Smits Professor of Cell Biology, California Institute of Technology

"Walsh effectively covers all of the major PTMs with a care for detail that is both admirable and captivating. The enzymes involved in generating PTMs are described with clarity and sufficient detail so that both novices and experts in this field are sure to learn much from this book."
—Benjamin F. Cravatt III, The Skaggs Institute for Chemical Biology, The Scripps Research Institute

"Walsh has coalesced the dizzying array of posttranslational modifications into a small subset of reactions. It is written with a concise chemical logic and Walsh’s typical flair that makes it a pleasure to read."
—Michael A. Marletta, Professor of Chemistry, Professor of Biochemistry and Molecular Biology, University of California, Berkeley

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Product Details

  • ISBN-13: 9780974707730
  • Publisher: Roberts and Company Publishers
  • Publication date: 10/28/2005
  • Edition description: 1st Edition
  • Edition number: 1
  • Pages: 576
  • Product dimensions: 10.30 (w) x 8.80 (h) x 1.30 (d)

Meet the Author

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.

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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

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