Hydrolytic enzymes:
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Amsterdam [u.a.]
Elsevier
1987
|
| Schriftenreihe: | New comprehensive biochemistry
16 |
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XII, 423 S. |
| ISBN: | 0444808868 0444803033 |
Internformat
MARC
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Datensatz im Suchindex
| _version_ | 1805082630565134336 |
|---|---|
| adam_text |
IMAGE 1
CONTENTS
PREFACE V
CHAPTER 1 ASPARTYLPROTEINASES, BY J.S. FRUTON (NEW HAVEN) 1
1. INTRODUCTION 1
(A) HISTORICAL BACKGROUND 1
(B) OCCURRENCE AND NOMENCLATURE 2
(C) PURIFICATION 3
(D) ASSAY 4
2. MOLECULAR PROPERTIES 5
(A) PHYSICAL-CHEMICAL PROPERTIES 5
(B) AMINO ACID COMPOSITION AND SEQUENCE 6
(C) CHEMICAL MODIFICATION 8
(D) PROTEIN-LIGAND INTERACTION 11
(E) DENATURATION 14
(0 THREE-DIMENSIONAL STRUCTURE 14
3. ACTION ON PROTEIN SUBSTRATES 15
(A) ACTIVATION OF ZYMOGENS . . 15
(B) CLEAVAGE OF PROTEIN SUBSTRATES 17
4. ACTION ON SYNTHETIC SUBSTRATES 19
(A) PRIMARY SPECIFICITY 19
(B) SECONDARY SPECIFICITY 22
(C) CONDENSATION REACTIONS 23
(D) TRANSPEPTIDATION REACTIONS 24
5. MECHANISM OF ACTION 25
(A) BINDING OF SUBSTRATE AT ACTIVE SITE 25
(B) TRANSITION STATE AND BOND CLEAVAGE 27
(C) RELEASE OF PRODUCTS 29
ACKNOWLEDGEMENT 30
REFERENCES 30
CHAPTER 2
CYSTEINE PROTEINASES, BY K. BROCKLEHURST, F. WILLENBROCK AND E. SALIH
(LONDON) 39
1. THE CYSTEINE PROTEINASES: GENERAL CONSIDERATIONS 39
(A) DEFINITION AND PRINCIPAL CATALYTIC SITE FEATURES 39
(B) THE ENZYMES, THEIR SOURCES, SIZES AND CHARGE CHARACTERISTICS 40
(C) ZYMOGENS 43
(D) THE CATALYSED REACTIONS: HYDROLYSIS AND PEPTIDE SYNTHESIS 45
(E) NATURALLY OCCURRING PEPTIDE INHIBITORS 48
IMAGE 2
VLLL
2. AN HISTORICAL PERSPECTIVE FROM PAPAINE TO CALPAIN 49
3. PHYSIOLOGICAL AND PATHOLOGICAL ASPECTS 58
4. ISOLATION AND ASSAY 62
(A) PURIFICATION 62
(B) CATALYTIC ACTIVITY 70
(C) ACTIVE SITE TITRATION 74
(D) IMMUNOLOGICAL TECHNIQUES 79
5. MOLECULAR STRUCTURE 80
(A) GENERAL COMMENTS ON THE THREE-DIMENSIONAL STRUCTURES OF CYSTEINE
PROTEINASES 80 (B) THE THREE-DIMENSIONAL STRUCTURE OF CALOTROPIN DI 82
(C) COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF PAPAIN AND
ACTINIDIN 83
(D) CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING 87
(E) OBSERVATIONS ON THE AMINO ACID SEQUENCES OF SOME CYSTEINE
PROTEINASES: PAPAIN, ACTINIDIN, STEM BROMELAIN, CATHEPSINS B AND H,
CHYMOPAPAINS A AND B, AND STREPTOCOCCAL PROTEINASE 91
6. SPECIFICITY 95
7. CHEMICAL MODIFICATION 101
(A) THE SCOPE OF THE TECHNIQUE 101
(B) GENERAL ASPECTS OF THE REACTIVITY PROBE APPROACH TO THE STUDY OF
ACTIVE CENTRE CHEMISTRY AND CATALYTIC MECHANISM 103
(C) STUDIES ON CYSTEINE PROTEINASES USING 2-PYRIDYL DISULPHIDES AS
TWO-PROTONIC-STATE REACTIVITY PROBES 105
(D) STUDIES USING OTHER TYPES OF REAGENT I LL
(E) NOVEL ENZYMES PRODUCED BY CHEMICAL MUTATION: FLAVOPAPAIN 115
8. SPECTROSCOPIC STUDIES 116
(A) THE RANGE OF SPECTROSCOPIC TECHNIQUES, THE PARTICULAR VALUE OF
VIBRATIONAL SPECTROSCOPY, AND A CAUTIONARY NOTE ABOUT ATTEMPTS TO
DETERMINE GROUP DISSOCIATION CONSTANTS OF INTERACTIVE SYSTEMS BY
SPECTROSCOPIC METHODS 116
(B) STUDIES ON CYSTEINE PROTEINASES 118
9. KINETICS AND CATALYTIC MECHANISM 124
(A) THE GENERAL PICTURE 124
(B) STRUCTURAL VARIATION IN THE CYSTEINE PROTEINASES AS AN AID TO THE
STUDY OF MECHANISM 125 (C) STRUCTURAL FEATURES OF PARTICULAR MECHANISTIC
SIGNIFICANCE 126
(D) THE MINIMAL KINETIC MECHANISM 127
(E) CATALYSIS AND SPECIFICITY 128
(0 THE ADSORPTIVE COMPLEX (ES) 129
(G) APPLICATION OF QSAR TO SUBSTRATE BINDING BY CYSTEINE PROTEINASES 129
(H) THE ACYLENZYME (THIOLESTER) INTERMEDIATE (ES') 129
(I) TETRAHEDRAL INTERMEDIATES AND TRANSITION STATE STABILISATION 131
(J) ACYLATION AND THE THIOL-IMIDAZOLE INTERACTIVE SYSTEM 134
(K) CONTROL OF CATALYTIC SITE GEOMETRY BY INTERACTIONS IN THE EXTENDED
BINDING AREAS 137 (1) DEACYLATION 138
(M) CYSTEINE PROTEINASE MECHANISM - A WORKING HYPOTHESIS 141
ACKNOWLEDGEMENTS 141
REFERENCES 143
CHAPTER 3 STRUCTURE AND FUNCTION OFSERINE PROTEASES, BY L. POLGAER
(BUDAPEST) 159
1. INTRODUCTION 159
2. THE PRE-CRYSTALLOGRAPHIC AGE 160
IMAGE 3
IX
(A) SERINE PROTEASES DESCENDED FROM ANCESTRAL GENES BY DIVERGENT AND
CONVERGENT EVOLUTION . 160
(B) MANY SERINE PROTEASES ARE SYNTHESIZED AS INACTIVE ZYMOGENS OR
PROENZYMES 160 (C) SERINE PROTEASES EXHIBIT BROAD SUBSTRATE
SPECIFICITIES 160
(D) THE ACTIVE SITE SERINE RESIDUE DISPLAYS UNIQUE REACTIVITY 162
(E) THE FORMATION OF A TRANSIENT ACYL-ENZYME IS SUPPORTED BY KINETIC
STUDIES 163
(F) A HISTIDINE SIDE CHAIN PARTICIPATES AS A GENERAL BASE CATALYST BOTH
IN THE FORMATION AND THE DECOMPOSITION OF THE ACYL-ENZYME 165
(G) THE OXYGEN NUCLEOPHILE (SERINE OR H 2O) REACTS IN ITS UNIONIZED FORM
166
(H) ACYLATION AND DEACYLATION ARE MECHANISTICALLY SYMMETRICAL PROCESSES
167
(I) THE TETRAHEDRAL INTERMEDIATE AND THE IMIDAZOLIUM ION CONSTITUTE A
CATALYTICALLY IMPORTANT ION-PAIR 168
3. STRUCTURAL FEATURES OF THE CATALYTIC MECHANISM 169
(A) THERE ARE CONSIDERABLE DIFFICULTIES IN ESTABLISHING THE PRECISE
STEREOCHEMISTRY OF THE CATALYSIS 169
(B) CRYSTALLOGRAPHIC STUDIES REVEALED AN CATALYTIC TRIAD AND AN OXYANION
BINDING SITE 170 (C) THE CATALYTIC SITES ARE VIRTUALLY IDENTICAL IN ALL
SERINE PROTEASES 171
(D) THE DIVERSITY OF SPECIFICITY IS PRINCIPALLY ASSOCIATED WITH THE
PRIMARY BINDING SITE OF SERINE PROTEASES 172
(E) SECONDARY SPECIFICITIES ARISE IN THE REACTIONS WITH POLYPEPTIDE
SUBSTRATES 174
(F) STRUCTURAL INFORMATION ABOUT THE LEAVING GROUP SIDE OF THE EXTENDED
BINDING SITE IS PROVIDED BY PROTEIN PROTEASE INHIBITORS 176
(G) THE S ' - P' INTERACTIONS PLAY AN IMPORTANT ROLE IN PEPTIDE BOND
SYNTHESIS MEDIATED BY SERINE PROTEASES 179
(H) TRANSITION STATE ANALOGUES MIMIC THE STRUCTURE OF THE TETRAHEDRAL
INTERMEDIATE 180 (I) AN APPROXIMATE STEREOCHEMISTRY OF THE CATALYSIS CAN
BE MODELED BY A COMBINATION OF X-RAY DIFFRACTION DATA AND CHEMICAL
CONSIDERATIONS 182
4. BEYOND THE STRUCTURE 185
(A) THE CATALYSIS IS HIGHLY SENSITIVE TO SMALL DISTORTIONS AT THE SIDE
OF THE TETRAHEDRAL INTERMEDIATE THAT FACES THE ENZYME 185
(B) TO WHAT EXTENT ARE THE TRANSITION STATE COMPLEX AND THE TETRAHEDRAL
INTERMEDIATE SIMILAR? 186
(C) THE CATALYTIC TRIAD MAY FUNCTION AS A CHARGE STABILIZING SYSTEM 191
5. CONCLUSION 192
ACKNOWLEDGEMENT 193
REFERENCES 193
CHAPTER 4 CARBOXYPEPTIDASE A, BY D.S. AULD AND B.L. VALLEE (BOSTON) 201
1. INTRODUCTION 201
2. STRUCTURAL PROPERTIES ?NI
(A) PRIMARY STRUCTURE 202
(B) TERTIARY STRUCTURE 204
3. CATALYTIC PROPERTIES 207
(A) REACTIONS CATALYZED 207
(B) THREE-PROTONATION-STATE MODEL 209
(C) CARBOXYLIC ACID INHIBITORS OF CATALYSIS 211
(D) TEMPERATURE-JUMP STUDIES OF THE ZINC ENZYME 213
4. CHEMICAL MODIFICATION OF ACTIVE SITE RESIDUES 214
(A) GLUTAMIC ACID 214
(B) TYROSINE 216
IMAGE 4
(C) ARGININE 220
(D) HISTIDINE 221
5. STRUCTURE-FUNCTION STUDIES BY SITE-DIRECTED MUTAGENESIS 221
6. FUNCTION OF THE METAL 222
7. THE CHROMOPHORIC COBALT ATOM AS AN ACTIVE SITE PROBE 227
8. CRYOSPECTROKINETIC STUDIES 232
(A) SUITABILITY OF CARBOXYPEPTIDASE A FOR CRYOSPECTROKINETIC STUDIES 232
(B) CRYOKINETICS OF ZINC AND COBALT ENZYMES 233
(C) OBSERVATION OF A PRE-STEADY-STATE AT SUBZERO TEMPERATURES 234
(D) THE QUESTION OF AN ACYL INTERMEDIATE 235
(E) CRYOSPECTROSCOPY OF COBALT CARBOXYPEPTIDASE A 237
(F) ELUCIDATION OF THE CHEMICAL NATURE OF THE ES 2 INTERMEDIATES 241
(G) REVERSIBILITY OF THE REACTION 243
9. HYDROLYSIS OF PEPTIDE SUBSTRATES 246
10. RATE DETERMINING STEP IN ESTER AND PEPTIDE HYDROLYSIS 248
11. RELATIONSHIP TO OTHER METALLOPROTEASES 249
12. SUMMARY 250
REFERENCES 250
CHAPTER 5
PROTEINASE INHIBITORS, BY Y. BIRK (REHOVOT) 257
1. INTRODUCTION 257
(A) GENERAL 257
(B) SCOPE AND PERSPECTIVES 258
2. DISTRIBUTION AND OCCURRENCE 260
3. CLASSIFICATION AND NOMENCLATURE 263
4. MECHANISM OF ACTION OF PROTEINASE INHIBITORS 264
(A) THE REACTIVE SITE 265
(B) THE STANDARD MECHANISM 265
5. PLANT PROTEINASE INHIBITORS 267
(A) GENERAL 267
(B) LEGUME SEED PROTEINASE INHIBITORS 268
(I) KUNITZ SOYBEAN TRYPSIN INHIBITOR (STI) FAMILY 268
(II) BOWMAN-BIRK PROTEINASE INHIBITOR (BBI) FAMILY 273
(C) POTATO PROTEINASE INHIBITORS 282
(I) PROTEINASE INHIBITOR I FAMILY 283
(II) PROTEINASE INHIBITOR II FAMILY 284
(III) CARBOXYPEPTIDASE INHIBITOR (CPI) 284
(IV) POLYPEPTIDE INHIBITORS OF SERINE PROTEINASES 285
(V) EFFECT OF FEEDING POTATO PROTEINASE INHIBITORS ON ANIMAL GROWTH 285
(D) WOUND-INDUCED PROTEINASE INHIBITORS IN PLANT LEAVES 286
(I) INHIBITORS OF SERINE PROTEINASES 286
(II) CARBOXYPEPTIDASE INHIBITOR (CPI) 287
(III) THE PROTEINASE INHIBITOR INDUCING FACTOR (PIIF) 287
(E) PROTEINASE INHIBITORS FROM OTHER PLANT SOURCES 288
(I) THE SQUASH FAMILY OF SERINE PROTEINASE INHIBITORS 288
(II) UNASSIGNED INHIBITORS 288
6. PROTEINASE INHIBITORS OF ANIMAL ORIGIN 290
(A) GENERAL 290
(B) PANCREATIC PROTEINASE INHIBITORS 290
X
IMAGE 5
XI
(I) BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) KUNITZ FAMILY 290
(II) PANCREATIC SECRETORY TRYPSIN INHIBITOR (PSTI) KAZAL FAMILY 294
(C) EGG WHITE PROTEINASE INHIBITORS 295
(I) OVOMUCOIDS 295
(II) OVOINHIBITORS 296
7. CONCLUDING REMARKS 299
ACKNOWLEDGEMENT 299
REFERENCES 300
CHAPTER 6 INTRACELLULAR PROTEOLYSIS, BY P. BOHLEY (TUEBINGEN) 307
1. INTRODUCTION 307
2. TURNOVER OF PROTEINS IN ORGANELLES 309
(A) PROTEIN TURNOVER IN NUCLEI 311
(B) PROTEIN TURNOVER IN MITOCHONDRIA 311
(C) PROTEIN TURNOVER IN LYSOSOMES 312
(D) PROTEIN TURNOVER IN PEROXISOMES 312
(E) PROTEIN TURNOVER IN THE MICROSOMAL FRACTION 312
(F) PROTEIN TURNOVER IN PLASMA MEMBRANES 313
(G) PROTEIN TURNOVER IN CYTOSOL 314
3. CELL PROTEINASES 315
(A) CATHEPSINS 315
(B) OTHER CELL PROTEINASES 315
(C) SPECIFICITY OF CELL PROTEINASES 315
(D) INHIBITORS 317
4. SUBSTRATE PROPERTIES DETERMINING PROTEOLYSIS IN CELLS 317
(A) ACETYLATION 318
(B) DEAMIDATION 318
(C) GLYCOSYLATION 318
(D) METHYLATION 319
(E) OXIDATION 319
(I) FORMATION OF MIXED DISULFIDES 319
(II) MIXED-FUNCTION OXIDATION OF HISTIDINE 319
(F) PHOSPHORYLATION 319
(G) UBIQUITINATION 320
(H) SURFACE HYDROPHOBICITY 320
5. REGULATION OF INTRACELLULAR PROTEOLYSIS 321
6. CONCLUDING REMARKS 322
ACKNOWLEDGEMENTS 323
REFERENCES 323
CHAPTER 7 PANCREATIC RIBONUCLEASE A: THE MOST STUDIED ENDORIBONUCLEASE,
BY M.R. EFTINK AND R.L. BILTONEN (UNIVERSITY AND CHARLOTTESVILLE) 333
1. INTRODUCTION 333
2. BIOLOGICAL FUNCTION AND OCCURRENCE OF RNASES 334
3. STRUCTURE OF RNASE A 335
(A) X-RAY AND NEUTRON DIFFRACTION STUDIES 335
IMAGE 6
XII
(B) NUCLEAR MAGNETIC RESONANCE STUDIES 340
4. THERMODYNAMICS OF LIGAND BINDING TO RNASE A 346
5. KINETICS 355
6. MISCELLANEOUS TOPICS 361
(A) THEORETICAL TREATMENTS 361
(B) SUBSITES 362
(C) GLYCOPROTEIN FORMS 364
7. SPECIFICITY, MECHANISM, AND ENERGETICS OF CATALYSIS 365
8. CONCLUDING REMARKS 371
REFERENCES 371
CHAPTER 8 PHOSPHOMONOESTERASES, BY J.E. COLEMAN AND M.J.A. BESMAN (NEW
HAVEN) 377
1. ZINC ALKALINE PHOSPHATASES. INTRODUCTION 377
2. ALKALINE PHOSPHATASE FROM ESCHERICHIA COLI 378
(A) BIOSYNTHESIS AND CELLULAR LOCATION 379
(B) PRIMARY AND THREE-DIMENSIONAL STRUCTURE 382
(C) KINETICS AND REACTION INTERMEDIATES OF ALKALINE PHOSPHATASE 384
(D) " 3CD-NMR AND X-RAY DIFFRACTION STUDIES 385
(E) "P-NMR APPLIED TO THE DETERMINATION OF STRUCTURE AND MECHANISM 389
(F) FUNCTIONAL CONSEQUENCES OF METAL ION SUBSTITUTIONS AT THE A- AND
B-SITES OF THE ACTIVE CENTER 392
(G) MECHANISM OF ACTION INCORPORATING CONCLUSIONS FROM THE MULTINUCLEAR
NMR DATA 394 (H) SITE-DIRECTED MUTAGENESIS OF E. COLI ALKALINE
PHOSPHATASE 395
3. MAMMALIAN ALKALINE PHOSPHATASES 396
4. ACID PHOSPHATASES FROM EUKARYOTES (LYSOSOMAL) 398
5. MANGANESE(III)-CONTAINING VIOLET ACID PHOSPHATASES 400
6. BINUCLEAR IRON-CONTAINING PURPLE ACID PHOSPHATASES, UTEROFERRINS 401
ACKNOWLEDGEMENT 403
REFERENCES 403
SUBJECT INDEX 407 |
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| series | New comprehensive biochemistry |
| series2 | New comprehensive biochemistry |
| spelling | Hydrolytic enzymes ed.: A. Neuberger ... Amsterdam [u.a.] Elsevier 1987 XII, 423 S. txt rdacontent n rdamedia nc rdacarrier New comprehensive biochemistry 16 Biochemistry Hydrolasen (DE-588)4160916-5 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Hydrolasen (DE-588)4160916-5 s DE-604 Neuberger, Albert 1908-1996 Sonstige (DE-588)1059253666 oth New comprehensive biochemistry 16 (DE-604)BV000003914 16 SWB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=000505538&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Hydrolytic enzymes New comprehensive biochemistry Biochemistry Hydrolasen (DE-588)4160916-5 gnd |
| subject_GND | (DE-588)4160916-5 (DE-588)4143413-4 |
| title | Hydrolytic enzymes |
| title_auth | Hydrolytic enzymes |
| title_exact_search | Hydrolytic enzymes |
| title_full | Hydrolytic enzymes ed.: A. Neuberger ... |
| title_fullStr | Hydrolytic enzymes ed.: A. Neuberger ... |
| title_full_unstemmed | Hydrolytic enzymes ed.: A. Neuberger ... |
| title_short | Hydrolytic enzymes |
| title_sort | hydrolytic enzymes |
| topic | Biochemistry Hydrolasen (DE-588)4160916-5 gnd |
| topic_facet | Biochemistry Hydrolasen Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=000505538&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| volume_link | (DE-604)BV000003914 |
| work_keys_str_mv | AT neubergeralbert hydrolyticenzymes |