Protein Lipidation
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Table of contents
- Contentsv
- Prefaceix
- Chapter 1. Mechanism of Catalysis by Protein Farnesyltransferase1
- I. Introduction to Protein Prenyltransferases: Protein Farnesyltransferase and Protein Geranylgerany1
- II. General Features of Protein Farnesyltransferase, a CaaX Prenyltransferase2
- III. Substrate Recognition by Protein Farnesyltransferase4
- IV. Kinetic Mechanism of Protein Farnesyltransferase7
- V. Chemical Mechanism of Protein Farnesyltransferase10
- VI. Concluding Remarks14
- References15
- Chapter 2. Structure of Protein Farnesyltransferase19
- I. Introduction20
- II. Structure21
- III. Mutagenesis Studies36
- IV. Inhibition of Catalytic Activity39
- V. Summary42
- References43
- Chapter 3. Mutational Analyses of Protein Farnesyltransferase47
- I. Introduction48
- II. Protein Farnesyltransferase49
- III. Deletion Studies50
- IV. Mutants Affecting Zinc Binding, Substrate Affinity, and Catalysis55
- V. Conversion of Protein Substrate Specificity65
- VI. Mutants Resistant to Farnesyltransferase Inhibitors74
- VII. Future Prospects76
- References78
- Chapter 4. Farnesyltransferase Inhibitors81
- I. Introduction81
- II. Early Inhibitors and Proof of Concept84
- III. Newer Compounds86
- IV. Transgenic Mouse Models in Development of Farnesyltransferase Inhibitors88
- V. Mechanisms of Apoptosis91
- VI. Non-Ras Targets92
- VII. Combinations of Farnesyltransferase Inhibitors with Other Therapeutics93
- VIII. Noncancer Apphcations94
- IX. Clinical Development of Farnesyltransferase Inhibitors95
- X. Conclusions97
- References97
- Chapter 5. Protein Geranylgeranyltransferase Type I105
- I. Introduction106
- II. Protein Geranylgeranyltransferase Type I107
- III. Future Prospects127
- References127
- Chapter 6. Biochemistry of Rab Geranylgeranyltransferase131
- I. Protein Prenylation131
- II. Identification of Geranylgeranylated Rab Proteins133
- III. Prenyl Acceptor: Rab Family of Proteins134
- IV. Identification and Isolation of Rab Geranylgeranyltransferase135
- V. Prenylation-Associated Factors: Rab Escort Protein Family136
- VI. Formation of Rab Escort Protein: Rab Complex137
- VII. Rab Geranylgeranyltransferase Genes and Primary Structure140
- VIII. Rab Geranylgeranyltransferase Three-Dimensional Structure141
- IX. Mechanism of Reaction: Binding of Geranylgeranyl Diphosphate143
- X. Mechanism of Reaction: Binding of Rab Escort Protein: Rab Complex144
- XL Mechanism of Reaction: Catalysis145
- XII. Membrane Association of Geranylgeranylated Rabs147
- XIII. Conclusions and Future Work149
- References150
- Chapter 7. Postisoprenylation Protein Processing: CXXX(CaaX) Endoproteoses and Isoprenylcysteine Cor155
- I. Introduction156
- II. Characterization of Isoprenylprotein Endoprotease Activities160
- III. Identification of Two Yeast Genes, AFCl (STE24) and RCEl, Involved in Endoproteolytic Processin167
- IV. Role for AFCl (SE24) in Proteolytic Processing of N Terminus of a-Factor in Saccharomyces cerevi173
- V. Characterization of Mammalian Orthologs for AFCI (STE24) and RCEl177
- VI. Modification of C-Terminal Isoprenylcysteine Residues by Methyl Esterification Reactions in CXXX187
- VII. Isoprenylation and Carboxyl Methylation in Proteins Containing Cys–Xaa–Cys and Cys–Cys Mo191
- VIII. Characterization of Yeast Protein Modification Catalyzed by STE14-Encoded Methyltransferase192
- IX. Methyl Esterification of Isoprenylated Mammalian Proteins198
- X. Conclusions207
- References209
- Chapter 8. Reversible Modification of Proteins with Thioester-Linked Fatty Acids215
- I. Introduction215
- II. Structural Requirements for Protein Thioacylation217
- III. Intracellular Sites of Thioacylation221
- IV. Thioacylating Activities224
- V. Mechanisms of Thioacylation226
- VI. Palmitoyl-Protein Thioesterases229
- VII. Future Prospects236
- References237
- Chapter 9. Biology and Enzymology of Protein N-Myristoylation241
- I. Introduction241
- II. Biology242
- III. Enzymology261
- IV. Prospectus285
- References286
- Author Index291
- Subject Index315
- Color Plate SectionColor Plate-1
This is the first compilation of protein lipidation enzymes. This volume summarizes recent dramatic developments regarding enzymes responsible for protein lipidation, a process critical for a number of physiological functions, including cell proliferation and morphology. Inhibitors of protein lipidation have recently been shown to be useful as anticancer drugs. Enzymatic mechanisms, mutational analysis, and structural studies are presented.
Key Features
* The enzymatic mechanisms of protein lipidation
* Three-dimensional structures of protein farnesytransferase, protein geranylgeranytransferase II, and n-myristoryltransferase
Key Features
* The enzymatic mechanisms of protein lipidation
* Three-dimensional structures of protein farnesytransferase, protein geranylgeranytransferase II, and n-myristoryltransferase