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Enzyme Kinetics and Mechanism, Part F: Detection and Characterization of Enzyme Reaction Intermediates de Daniel L. Purich

Enzyme Kinetics and Mechanism, Part F: Detection and Characterization of Enzyme Reaction Intermediates: Methods in Enzymology, cartea 354

Autor Daniel L. Purich
en Limba Engleză Hardback – 4 noi 2002
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
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Specificații

ISBN-13: 9780121822576
ISBN-10: 0121822575
Pagini: 650
Dimensiuni: 152 x 229 x 27 mm
Greutate: 0.84 kg
Editura: ELSEVIER SCIENCE
Seria Methods in Enzymology

Public țintă

Biochemists, biophysicists, pharmacologists, molecular biologists, analytical, organic, and medicinal chemists, and graduate students in these disciplines

Cuprins


Covalent Enzyme-Substrate Compounds: Detection and Catalytic Competence.
Rapid Mix-Quench MALDI-TOF Mass Spectrometry for Analysis of Enzymatic Systems.
Pre-Steady-State Kinetics of Enzymatic Reactions Studied by Electrospray Mass Spectrometry with On-Line Rapid-Mixing Techniques.
Trapping of -Glycosidase Intermediates.
Trapping Covalent Intermediates on ß-Glycosidases.
2-Hydroxy-6-keto-nona-2,4-diene 1,9-Dioic Acid 5,6-Hydrolase: Evidence from18O Isotope Exchange for gem-Diol Intermediate.
Nucleoside-Diphosphate Kinase: Structural and Kinetic Analysis of Reaction Pathway and Phosphohistidine Intermediate.
Galactose-1-Phosphate Uridylyltransferase: Kinetics of Formation and Reaction of Uridylyl-Enzyme Intermediate in Wild-Type and Specifically Mutated Uridylyltransferases.
Kinetic Evidence for Covalent Phosphoryl-Enzyme Intermediate in Phosphotransferase Activity of Human Red Cell Pyrimidine Nucleotidases.
Characterization of (2->6) -Sialyltransferase Reaction Intermediates: Use of Alternative Substrates to Unmask Kinetic Isotope Effects.
Use of Sodium Borohydride to Detect Acyl-Phosphate Linkages in Enzyme Reactions.
Evidence for Phosphotransferases Phosphorylated on Aspartate Residue in N-Terminal DXDX(T/V) Motif.
MurC and MurD Synthetases of Peptidoglycan Biosynthesis: Borohydride Trapping of Acyl-Phosphate Intermediates.
Transaldolase B: Borohydride Reduction Trapping of Schiff Base Intermediate between Dihydroxyacetone and -Amino Group of Active-Site Lysine Residue.
Use of NMR and Borohydride Trapping to Provide Evidence for Covalent Enzyme-Substrate Imine Intermediate.
Detection of Covalent Tetrahedral Adducts by Differential Isotope Shift ¹³C NMR: Acetyl-Enzyme Reaction Intermediate Formed by 3-Hydroxy-3-methylglutaryl-CoA Synthase.
Detection of Intermediates in Reactions Catalyzed by PLP-Dependent Enzymes: O-Acetylserine Sulfhydrylase and Serine-Glyoxalate Aminotransferase.
Protein Tyrosine Phosphatase: X-Ray Crystallographic Observation of Cysteinyl-Phosphate Reaction Intermediate.
GTP:GTP Guanylyltransferase: Trapping Procedures for Detecting and Characterizing Chemical Nature of Enzyme-Nucleotide Phosphoramidate Reaction Intermediate.
-Glutamyl Thioester Intermediate in Glutaminase Reaction Catalyzed by Escherichia coli Asparagine Synthetase B.
-Glutamyltranspeptidase and -Glutamyl Peptide Ligases: Fluorophosphonate and Phosphonodifluoromethyl Ketone Analogs as Probes of Tetrahedral Transition State and -Glutamyl-Phosphate Intermediate.
Stoichiometric Redox Titrations of Complex Metalloenzymes.
Urate Oxidase: Single-Turnover Stopped-Flow Techniques for Detecting Two Discrete Enzyme-Bound Intermediates.
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.
Myeloperoxidase: Kinetic Evidence for Formation of Enzyme-Bound Chlorinating Intermediate.
Time-Resolved Resonance Raman Spectroscopy of Intermediates in Cytochrome Oxidase.
Porphobilinogen Deaminase: Accumulation and Detection of Tetrapyrrole Intermediates Using Enzyme Immobilization.
Adenosylcobalamin-Dependent Glutamate Mutase: Pre-Steady-State Kinetic Methods for Investigating Reaction Mechanism.
Ribonucleotide Reductase: Kinetic Methods for Demonstrating Radical Transfer Pathway in Protein R2 of Mouse Enzyme in Generation of Tyrosyl Free Radical.
Galactose Oxidase: Probing Radical Mechanism with Ultrafast Radical Probe.
Kinetic Characterization of Transient Free Radical Intermediates in Reaction of Lysine 2,3-Aminomutase by EPR Lineshape Analysis.
Demonstration of Peroxodiferric Intermediate in M-Ferritin Ferroxidase Reaction Using Rapid Freeze-Quench Mössbauer, Resonance Raman, and XAS Spectroscopies.
A Survey of Covalent, Ionic, and Radical Intermediates in Enzyme-Catalyzed Reactions.

Recenzii

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