Purich Enzyme Kinetics and Mechanism, Part F: Detection and Characterization of Enzyme Reaction Intermediates

1. Auflage 2002
ISBN: 978-0-08-048938-4
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 354, 650 Seiten

Reihe: Methods in Enzymology

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today-truly an essential publication for researchers in all fields of life sciences. - Spectroscopic Detection of Reaction Intermediates - Isotopic and Kenetic Detection of Reaction Intermediates - Chemical Trapping and Inhibitor Methods for Detecting Reaction Intermediates

Daniel Lee Purich has been at the forefront of biochemistry research for more than 25 years. He was awarded the National Institutes of Health Research Career Development Award from 1977-1982, the Plous Teaching Award (the University of California Santa Barbara Campus-Wide Teaching Award) in 1977, has been a member of the National Institutes of Health Biochemistry Study Section from 1982-1985, and a member of the Journal of Biological Chemistry Editorial Board from 1981-1986. He has been a member of the American Society of Biological Chemists, the American Chemical Society, the New York Academy of Sciences, the Biochemical Society, and the American Society for Cell Biology. Dr. Purich is currently a Professor and Chairman of the Department of Biochemistry and Molecular Biology at the Florida College of Medicine. He is the author and editor of numerous scientific publications.

Autoren/Hrsg.

Purich, Daniel L.

Inhaltsverzeichnis

1;Cover;1
2;Table of Contents;6
3;CONTRIBUTORS TO VOLUME 354;10
4;Preface;14
5;Volumes in Series;16
6;Chapter 1. Covalent Enzyme–Substrate Compounds: Detection and Catalytic Competence;37
7;Chapter 2. Rapid Mix-Quench MALDI-TOF Mass Spectrometry for Analysis of Enzymatic Systems;63
8;Chapter 3. Pre-Steady-State Kinetics of Enzymatic Reactions Studied by Electrospray Mass Spectrometry with On-Line Rapid-Mixing Techniques;86
9;Chapter 4. Trapping of a-Glycosidase Intermediates;100
10;Chapter 5. Trapping Covalent Intermediates on ß-Glycosidases;120
11;Chapter 6. 2-Hydroxy-6-keto-nona-2,4-diene 1,9-Dioic Acid 5,6-Hydrolase: Evidence from 18O Isotope Exchange for gem-Diol Intermediate;142
12;Chapter 7. Nucleoside-Diphosphate Kinase: Structural and Kinetic Analysis of Reaction Pathway and Phosphohistidine Intermediate;154
13;Chapter 8. Galactose-1-Phosphate Uridylyltransferase: Kinetics of Formation and Reaction of Uridylyl- Enzyme Intermediate inWild-Type and Specifically Mutated Uridylyltransferases;170
14;Chapter 9. Kinetic Evidence for Covalent Phosphoryl- Enzyme Intermediate in Phosphotransferase Activity of Human Red Cell Pyrimidine Nucleotidases;185
15;Chapter 10. Characterization of a(2„>6)-Sialyltransferase Reaction Intermediates: Use of Alternative Substrates to Unmask Kinetic Isotope Effects;195
16;Chapter 11. Use of Sodium Borohydride to Detect Acyl-Phosphate Linkages in Enzyme Reactions;204
17;Chapter 12. Evidence for Phosphotransferases Phosphorylated on Aspartate Residue in N-Terminal DXDX(T/V) Motif;213
18;Chapter 13. MurC and MurD Synthetases of Peptidoglycan Biosynthesis: Borohydride Trapping of Acyl- Phosphate Intermediates;225
19;Chapter 14. Transaldolase B: Trapping of Schiff Base Intermediate between Dihydroxyacetone and e-Amino Group of Active-Site Lysine Residue by Borohydride Reduction;233
20;Chapter 15. T4 Endonuclease V: Use of NMR and Borohydride Trapping to Provide Evidence for Covalent Enzyme–Substrate Imine Intermediate;238
21;Chapter 16. Detection of Covalent Tetrahedral Adducts by Differential Isotope Shift 13C NMR: Acetyl- Enzyme Reaction Intermediate Formed by 3-Hydroxy-3-methylglutaryl-CoA Synthase;244
22;Chapter 17. Detection of Intermediates in Reactions Catalyzed by PLP-Dependent Enzymes: O-Acetylserine Sulfhydrylase and Serine–Glyoxalate Aminotransferase;259
23;Chapter 18. Protein Tyrosine Phosphatases: X-Ray Crystallographic Observation of Cysteinyl-Phosphate Reaction Intermediate;273
24;Chapter 19. GTP:GTP Guanylyltransferase: Trapping Procedures for Detecting and Characterizing Chemical Nature of Enzyme–Nucleotide Phosphoramidate Reaction Intermediate;287
25;Chapter 20. .-Glutamyl Thioester Intermediate in Glutaminase Reaction Catalyzed by Escherichia coli Asparagine Synthetase B;296
26;Chapter 21. .-Glutamyltranspeptidase and .-Glutamyl Peptide Ligases: Fluorophosphonate and Phosphonodifluoromethyl Ketone Analogs as Probes of Tetrahedral Transition State and .-Glutamyl- Phosphate Intermediate;308
27;Chapter 22. Stoichiometric Redox Titrations of Complex Metalloenzymes;332
28;Chapter 23. Urate Oxidase: Single-Turnover Stopped-Flow Techniques for Detecting Two Discrete Enzyme-Bound Intermediates;346
29;Chapter 24. Nitric Oxide Synthase: Use of Stopped-Flow Spectroscopy and Rapid-Quench Methods in Single-Turnover Conditions to Examine Formation and Reactions of Heme–O2 Intermediate in Early Catalysis;356
30;Chapter 25. Myeloperoxidase: Kinetic Evidence for Formation of Enzyme-Bound Chlorinating Intermediate;374
31;Chapter 26. Time-Resolved Resonance Raman Spectroscopy of Intermediates in Cytochrome Oxidase;387
32;Chapter 27. Porphobilinogen Deaminase: Accumulation and Detection of Tetrapyrrole Intermediates Using Enzyme Immobilization;404
33;Chapter 28. Adenosylcobalamin-Dependent Glutamate Mutase: Pre-Steady-State Kinetic Methods for Investigating Reaction Mechanism;416
34;Chapter 29. Ribonucleotide Reductase: Kinetic Methods for Demonstrating Radical Transfer Pathway in Protein R2 of Mouse Enzyme in Generation of Tyrosyl Free Radical;435
35;Chapter 30. Galactose Oxidase: Probing Radical Mechanism with Ultrafast Radical Probe;451
36;Chapter 31. Kinetic Characterization of Transient Free Radical Intermediates in Reaction of Lysine 2,3- Aminomutase by EPR Lineshape Analysis;462
37;Chapter 32. Demonstration of Peroxodiferric Intermediate in M-Ferritin Ferroxidase Reaction Using Rapid Freeze-Quench Mössbauer, Resonance Raman, and XAS Spectroscopies;472
38;Chapter 33. A Survey of Covalent, Ionic, and Radical Intermediates in Enzyme-Catalyzed Reactions;491
39;AUTHOR INDEX;507
40;SUBJECT INDEX;539