Christov Metal-Containing Enzymes

1. Auflage 2014
ISBN: 978-0-12-800788-4
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 97, 174 Seiten

Reihe: Advances in Protein Chemistry and Structural Biology

Published continuously since 1944, the Advances in Protein Chemistry and Structural Biology series is the essential resource for protein chemists. Each volume brings forth new information about protocols and analysis of proteins. Each thematically organized volume is guest edited by leading experts in a broad range of protein-related topics. - Describes advances in metal-containing enzymes - Chapters are written by authorities in their field - Targeted to a wide audience of researchers, specialists, and students - The information provided in the volume is well supported by a number of high quality illustrations, figures, and tables

Autoren/Hrsg.

Christov, Christo

Inhaltsverzeichnis

1;Front Cover;1
2;Metal-Containing Enzymes;4
3;Copyright;5
4;Contents;6
5;Contributors;8
6;Preface;10
7;Chapter 1: Type-3 Copper Proteins: Recent Advances on Polyphenol Oxidases;12
7.1;1. Introduction;13
7.2;2. Primary Structure and Molecular Weights of PPOs;18
7.2.1;2.1. General sequence structure;18
7.2.2;2.2. Core domain, C-terminal domain, and its proteolytic cleavage site;18
7.2.3;2.3. Conserved amino acid motifs in the core domain;19
7.2.4;2.4. Conserved amino acid motifs in the C-terminal domain;20
7.2.5;2.5. Transit peptide and location of PPOs;20
7.2.6;2.6. Sequence homologies within PPOs;22
7.2.7;2.7. In vitro activation of PPOs;27
7.2.8;2.8. In vivo activation of PPOs;27
7.2.9;2.9. Mutants of PPOs;27
7.2.9.1;2.9.1. Mutants of plant PPOs;27
7.2.9.2;2.9.2. Mutants of fungal PPOs;27
7.2.9.3;2.9.3. Mutants of bacterial PPOs;28
7.3;3. Oxo Complex;28
7.3.1;3.1. Oxo complex investigated by UV/vis absorption spectroscopy;29
7.3.2;3.2. Oxo complex investigated by CD spectroscopy;29
7.3.3;3.3. Oxo complex investigated by resonance Raman spectroscopy;29
7.3.4;3.4. Oxo complex of catechol oxidase;30
7.3.5;3.5. Oxo complex of tyrosinase;30
7.3.6;3.6. Oxo complex of aureusidin synthase;33
7.3.7;3.7. Oxo complex of hemocyanin;33
7.4;4. X-ray Crystallographic Structural Data of PPOs and Hemocyanins;33
7.4.1;4.1. Published structures in the protein data bank;33
7.4.1.1;4.1.1. Published structures in the PDB of hemocyanins;33
7.4.1.2;4.1.2. Published structures in the PDB of catechol oxidases;33
7.4.1.3;4.1.3. Published structures in the PDB of tyrosinases;38
7.4.2;4.2. Structural differences of tyrosinases and catechol oxidases;40
7.5;5. Conclusions and Outlook;41
7.6;Acknowledgments;41
7.7;References;41
8;Chapter 2: Biophysical Studies of Matrix Metalloproteinase/Triple-Helix Complexes;48
8.1;1. MMPs and Collagen Hydrolysis;48
8.2;2. Structures of Full-Length, Collagenolytic MMPs in Solution and in the Solid State;49
8.3;3. Structural Evaluation of MMP Interactions with Collagen;52
8.4;4. Mechanism of Collagenolysis;54
8.5;5. Heterogeneity in MMP Structures;57
8.6;Acknowledgment;58
8.7;References;58
9;Chapter 3: Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions;60
9.1;1. Introduction;61
9.2;2. Metallo-ß-Lactamases, Major Culprits in the Emergence of Antibiotic Resistance;61
9.3;3. Methionine Aminopeptidase, a Target for Novel Anticancer Drugs;68
9.4;4. Glycerophosphodiesterase, a Very Promiscuous Potential Bioremediator;71
9.5;5. PAP, an Alternative Target to Treat Osteoporosis;76
9.6;6. Conclusions and Outlook: Agmatinase, an Emerging Target for Biotechnological Applications;80
9.7;Acknowledgments;82
9.8;References;83
10;Chapter 4: Applications of Quantum Mechanical/Molecular Mechanical Methods to the Chemical Insertion Step of DNA and RNA ...;94
10.1;1. Introduction;96
10.2;2. Methods for Describing Reactive Pathways;96
10.3;3. DNA Polymerase ß;98
10.3.1;3.1. Abashkin, Erickson, and Burt (2001): A cluster QM calculation at steps along a proposed reaction path;98
10.3.2;3.2. Rittenhouse, Apostoluk, Miller, and Straatsma (2003): A cluster QM calculation on the prechemistry complex of Pol ß;100
10.3.3;3.3. Sawaya et al., 1997);100
10.3.4;3.4. Batra et al., 2006);101
10.3.5;3.5. Batra et al., 2008);105
10.3.6;3.6. Batra et al. (2013): A QM/MM study based on the X-ray crystal structure of the Pol ß variant D256E;106
10.3.7;3.7. The broader picture: Pol ß;108
10.4;4. Application of QM/MM to Systems Similar to Pol ß;109
10.4.1;4.1. Pol . insertion;109
10.4.2;4.2. Dpo4 insertion;111
10.4.3;4.3. Pol . insertion;112
10.5;5. RNA Polymerase;114
10.6;6. Thoughts for Future QM/MM Simulations on Ternary Substrate Complexes of Nucleic Acid Polymerases;117
10.7;7. Conclusions;120
10.8;Acknowledgments;120
10.9;References;120
11;Chapter 5: Monitoring the Biomolecular Interactions and the Activity of Zn-Containing Enzymes Involved in Conformational ...;126
11.1;1. Zn-Metalloproteases and Conformational Diseases;127
11.2;2. Analytical Techniques Used to Study ZnMPs-Substrate/Inhibitors Interactions;131
11.2.1;2.1. Studying ZnMPs at atomic level;132
11.2.1.1;2.1.1. Nuclear magnetic resonance;132
11.2.1.2;2.1.2. X-ray crystallography;134
11.2.2;2.2. Analytical techniques able to provide information on binding affinities, activities, and substrate-induced conformat...;136
11.2.2.1;2.2.1. Surface plasmon resonance;136
11.2.2.2;2.2.2. Other optical methods;138
11.2.3;2.3. Mass spectrometry and ZnMPs;142
11.3;3. Conclusions and Future Perspectives;146
11.4;References;146
12;Author Index;154
13;Subject Index;170