Posttranslational Modification of Proteins: Expanding Nature's Inventory

Front Cover
Roberts and Company Publishers, 2006 - Science - 490 pages
0 Reviews
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.
 

What people are saying - Write a review

We haven't found any reviews in the usual places.

Contents

Introduction
1
Swinging Arms for Him in Lipoate and Phosphopantetheine Tethering
14
Protein Phosphorylation by Protein Kinases
35
Action of Protein Sulfotransferases and Aryl Sulfatases
81
Modifications of Cysteine and Methionine by OxidationReduction
95
Protein Methylation
121
Protein NMethylation 13 2
132
Protein NAcetylation
151
Protein Glycosylation
281
NLinked Glycoproteins
291
Cycles
298
OGlycosylation of Proteins
305
Protein CGlycosylation
311
ADPRibosylation of Proteins from NAD as Donor
317
Posttranslational Hydroxylation of Proteins
331
Protein Automodification Reactions
349

Protein Lipidation
171
Proteolytic Posttranslational Modification of Proteins
203
Ubiquitin and Ubiquitinlike Protein Tags
243
Sorting in the Cell
258
The Beginnings of a Proteomics Approach to Define the Full Range
275
Swinging Arms for Biotin Lipoate and Phosphopantetheine Tethering
405
Protein Carboxylation and Amidation 43 5
435
Diversification of Proteomes
461
Index
477
Copyright

Common terms and phrases

About the author (2006)

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.

Bibliographic information