Posttranslational modification of proteins : expanding nature's inventory
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Bibliographic Information
Posttranslational modification of proteins : expanding nature's inventory
Roberts and Co. Publishers, c2006
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Note
Includes bibliographical references and index
Description and Table of Contents
Description
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.
Table of 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
by "Nielsen BookData"