Molecular aspects of enzyme catalysis:
Saved in:
| Format: | Book |
|---|---|
| Language: | English |
| Published: |
Tokyo
Kodansha u.a.
1994
|
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XIV, 244 S. Ill., graph. Darst. |
| ISBN: | 3527300171 1560817119 4062064979 |
Staff View
MARC
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| 245 | 1 | 0 | |a Molecular aspects of enzyme catalysis |c ed. by Toshio Fukui ... |
| 264 | 1 | |a Tokyo |b Kodansha u.a. |c 1994 | |
| 300 | |a XIV, 244 S. |b Ill., graph. Darst. | ||
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| 650 | 4 | |a Biological control systems | |
| 650 | 4 | |a Catalysis | |
| 650 | 4 | |a Enzyme Activation | |
| 650 | 4 | |a Enzymes | |
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Record in the Search Index
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| adam_text | Contents
Dedication v
List of Contributors vii
Preface xv
Frontispiece xvii
Introduction—New Trends in Enzyme Studies 1
Enzyme Purification 1
Enzyme Structure 3
Enzyme Reaction Mechanisms 6
Novel Enzymes 8
Enzyme Applications 10
Perspectives 11
References 12
1. Advanced Protein Sequencing Techniques 15
1.1 Introduction 15
1.2 The Primary Structure of Aspartate Aminotransferase (AspAT) 17
1.3 Progress in Primary Structure Analysis 20
1.3.1 Direct Sequencing of Protein 20
1.3.2 A Sequencing Approach Based on cDN A 30
1.3.3 Application of Mass Spectrometry to Protein Primary Sequence Determination
32
1.3.4 Database 33
1.4 Conclusions 33
References 34
2. Nuclear Magnetic Resonance Studies on Streptomyces Subtilisin Inhibitor
and its Complexes with Proteinases 37
2.1 Introduction 37
2.2 Assignment of the Backbone Peptide Carbonyl Carbon BCNMR Signals for
Larger Proteins 39
2.3 Structural Elucidation of the Stable Intermediate for the SSI Subtilisin System
by 13C NMR Spectroscopy 41
ix
x Contents
2.4 Facile Restoration of the Hydrolyzed Scissile Bond of SSI* in the Subtilisin
Complex 45
2.5 Global Conformational Changes of SSI Induced by Complex Formation with
Subtilisin 47
2.6 Conformations of the Flexible Segments of Domain II and the Topology of
Proteinase Surface are Interdependent 49
2.7 Summary and Conclusion 51
References 52
3. Subunit Assembly of Oligomeric Enzymes 55
3.1 Introduction 55
3.2 Functional Roles of Subunit Assembly and Disassembly 55
3.3 Determination of Composition and Geometric Arrangements of Subunits 57
3.4 Determination of Subunit Contact Regions and Strength of Subunit
Interactions 58
3.4.1 Identification of Subunit Contact Regions 58
3.4.2 Evaluation of the Strength of Interactions Between Subunits 59
3.5 Experimental Approaches to Reveal the Relationship Between Oligomeric
Structure and Biological Activity 61
3.5.1 Analysis of Dissociation and Association Processes in Oligomeric Proteins 61
3.5.2 Hybridization Experiments 61
3.5.3 Site directed Mutagenesis at the Subunit Interface 66
3.5.4 Analysis of Subunit Association and Dissociation in the Cell 66
3.6 Proteins Involved in Subunit Assembly in vivo 66
3.6.1 Molecular Chaperones 66
3.6.2 Other Proteins Involved in Subunit Assembly 69
3.7 Conclusion 69
References 70
4. Affinity Labeling of Nucleotide Binding Sites 73
4.1 Introduction 73
4.2 Nucleoside Polyphosphopyridoxals (NPn PL) 75
4.2.1 Synthesis 75
4.2.2 Inactivation Kinetics 75
4.2.3 Identification of Labeled Sites 76
4.3 Case Studies 76
4.3.1 Glycogen Synthase 76
4.3.2 Adenylate Kinase 77
4.3.3 UDP Glucose Pyrophosphorylase 78
4.3.4 Fi ATPase 81
4.3.5 Ion Transporting ATPases 82
4.3.6 Protein Kinases 83
Contents xi
4.4 Concluding Remarks 84
References 85
5. Structure and Function of Aspartate Aminotransferase 87
5.1 Introduction 87
5.2 Background 87
5.3 Site directed Mutagenesis on AspAT 93
5.4 X ray Crystallographic Study on AspAT 93
5.5 Evaluation of the Active Site Residues in AspAT by in vitro Mutagenesis 94
5.5.1 Lys 258 and Tyr 70* 95
5.5.2 Tyr 225 97
5.5.3 Asp 222 and His 143 98
5.5.4 Arg 292* and Arg 386 98
5.5.5 Trp 140 99
5.5.6 Cys Residues 99
5.6 Substrate Binding Pocket 101
5.7 Future Prospects 104
References 104
6. Higher Plant Phosphorylases 107
6.1 Introduction 107
6.2 Phosphorylase Isozymes from Higher Plants 108
6.3 Structures of Phosphorylase Isozymes from Potato Tuber 109
6.3.1 Type L Isozyme 109
6.3.2 Type H Isozyme 111
6.3.3 Sequence Comparison and Stereostructure 113
6.3.4 Functional Role of the 78 Residue Insertion in Type L Isozyme 119
6.4 Catalytic Mechanism 120
6.5 Evolution of Plant Phosphorylases 122
6.6 Concluding Remarks 123
References 123
7. Tryptophan Synthase 127
7.1 Introduction 127
7.2 Structure and Function of the a Subunit 128
7.2.1 Structure 128
7.2.2 Active Site Residues 129
7.2.3 Flexible Loop 130
7.2.4 Protein Folding and Stability 131
xii Contents
7.3 Structure and Function of the /? Subunit 131
7.3.1 Structure and Domains 131
7.3.2 Pyridoxal Phosphate Intermediates 133
7.3.3 Active Site Residues 133
7.4 The Indole Tunnel and Indole Channeling 138
7.5 Interactions Between the a and /? Subunits 140
7.6 Reciprocal Communication Between the a and /? Subunits 141
7.7 Catalytic Mechanism of the Physiological a/3 Reaction 142
7.8 Unanswered Questions and Future Directions 142
References 144
8. Alanine Racemase:
Structure and Functions 147
8.1 Physiological Function of Alanine Racemase 147
8.2 Genetical and Evolutional Aspects of Alanine Racemase 148
8.3 Structure of Thermostable Alanine Racemase of Bacillusstearothermophilus 150
8.3.1 Subunit Dissociation and Unfolding 150
8.3.2 Limited Proteolysis 152
8.3.3 Construction and Expression of Fragmentary Enzyme 152
8.3.4 Unfolding and Reconstitution of Fragmentary Enzyme 154
8.4 Reaction Mechanism of Alanine Racemase 155
8.5 Inhibitors of Alanine Racemase 159
References 162
9. Tryptophanase:
Structural, Spectral, and Catalytic Properties 165
9.1 Introduction 165
9.2 Structural Properties 166
9.2.1 Primary and Quaternary Structure 166
9.2.2 Unfolding and Refolding 170
9.3 Spectral Properties of the Free Enzyme and Catalytic Intermediates 172
9.3.1 Absorption Spectra 172
9.3.2 Circular Dichroism 174
9.3.3 Fluorescence 177
9.3.4 NMR Spectra 178
9.4 Chemical Modification and Site Directed Mutagenesis 179
9.5 Catalytic Properties 182
9.5.1 Activation by Cations 182
9.5.2 Coenzyme Reorientations in the Active Site 183
9.5.3 Catalytic Mechanism 186
References 188
k
I
Contents xiii
10 Superoxide Dismutase 191
10.1 Introduction 191
10.2 Distribution of SOD among Organisms 192
10.2.1 Phylogenic Distribution 192
10.2.2 Subcellular Localization 192
10.3 Physiological Functions 193
10.3.1 Defense against Oxygen Toxicity 193
10.3.2 Gene Regulation 194
10.4 Molecular Properties 195
10.4.1 CuZn SOD 195
10.4.2 Fe SOD and Mn SOD 200
10.5 Properties of Superoxide Radical and Analytical Methods 201
10.5.1 Superoxide Anion Radical as a Substrate 202
10.5.2 Diffusion controlled Reaction 202
10.5.3 Assay of SOD 202
10.6 Kinetics and Reaction Mechanisms 204
10.6.1 CuZn SOD 204
10.6.2 Fe SOD and Mn SOD 207
10.6.3 Inactivation by H2O2 208
References 209
11. H+ ATPase:
Catalysis and H+Translocation 211
11.1 Introduction 211
11.2 Structure and Function of F type ATPase 213
11.2.1 Preparation of F0F1 213
11.2.2 Assembly and Structure of F0F1 214
11.2.3 Uni site and Multi site Catalysis by Fi 216
11.3 Catalytic Site of F type ATPase 217
11.3.1 Affinity Labeling of Catalytic Site of F, ATPase 217
11.3.2 Mutations in the Glycine rich Sequence 219
11.3.3 Amino Acid Resides Interacting with Glycine rich Sequence 220
11.4 Pathway and Regulation of H+ Transport 221
11.4.1 Assembly of Fo 221
11.4.2 Proton Pathway in Fo 221
11.4.3 Regulation of Proton Conduction 225
11.5 Conclusion 226
References 226
f
xiv Contents
12. Stabilization of Proteases by an Engineered Disulfide Bond 229
12.1 Aqualysin I is a Thermostable Protease 230
12.2 Aqualysin I Belongs to a Family of Subtilisin type Serine Proteases 230
12.3 Comparison of Known Three dimensional Structures of Subtilisin type Serine
Proteases: Probable Structural Similarity Between Aqualysin I and Other
Subtilisin type Enzymes 232
12.4 Aqualysin I Contains Two Disulfide Bonds 232
12.5 Introduction of a Disulfide Bond into Subtilisin by Site directed Mutagenesis
234
12.5.1 Mutant Subtilisin E Having a Cys61 Cys98 Disulfide Bond Gains Thermo¬
stability 234
12.5.2 Another Mutant Did Not Form Disulfide Linkage 237
12.6 Other Attempts to Increase the Thermostability of Subtilisin are Unsuccessful
237
12.7 Another Example, an Alkaline Protease from Aspergillus oryzae 237
12.8 Conclusions 238
References 238
Index 241
k
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| indexdate | 2024-07-09T17:31:28Z |
| institution | BVB |
| isbn | 3527300171 1560817119 4062064979 |
| language | English |
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| spelling | Molecular aspects of enzyme catalysis ed. by Toshio Fukui ... Tokyo Kodansha u.a. 1994 XIV, 244 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Biological control systems Catalysis Enzyme Activation Enzymes Enzymes Regulation Enzym (DE-588)4014988-2 gnd rswk-swf Enzymkatalyse (DE-588)4152480-9 gnd rswk-swf Biokatalysator (DE-588)4006842-0 gnd rswk-swf Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Enzymkatalyse (DE-588)4152480-9 s DE-604 Enzym (DE-588)4014988-2 s Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 s Biokatalysator (DE-588)4006842-0 s Fukui, Toshio Sonstige oth HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=006051216&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Molecular aspects of enzyme catalysis Biological control systems Catalysis Enzyme Activation Enzymes Enzymes Regulation Enzym (DE-588)4014988-2 gnd Enzymkatalyse (DE-588)4152480-9 gnd Biokatalysator (DE-588)4006842-0 gnd Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 gnd |
| subject_GND | (DE-588)4014988-2 (DE-588)4152480-9 (DE-588)4006842-0 (DE-588)4183784-8 (DE-588)4143413-4 |
| title | Molecular aspects of enzyme catalysis |
| title_auth | Molecular aspects of enzyme catalysis |
| title_exact_search | Molecular aspects of enzyme catalysis |
| title_full | Molecular aspects of enzyme catalysis ed. by Toshio Fukui ... |
| title_fullStr | Molecular aspects of enzyme catalysis ed. by Toshio Fukui ... |
| title_full_unstemmed | Molecular aspects of enzyme catalysis ed. by Toshio Fukui ... |
| title_short | Molecular aspects of enzyme catalysis |
| title_sort | molecular aspects of enzyme catalysis |
| topic | Biological control systems Catalysis Enzyme Activation Enzymes Enzymes Regulation Enzym (DE-588)4014988-2 gnd Enzymkatalyse (DE-588)4152480-9 gnd Biokatalysator (DE-588)4006842-0 gnd Struktur-Aktivitäts-Beziehung (DE-588)4183784-8 gnd |
| topic_facet | Biological control systems Catalysis Enzyme Activation Enzymes Enzymes Regulation Enzym Enzymkatalyse Biokatalysator Struktur-Aktivitäts-Beziehung Aufsatzsammlung |
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