Pyridine Nucleotide-Dependent Dehydrogenases
Springer-Verlag Berlin and Heidelberg GmbH & Co. K
978-3-540-04988-3 (ISBN)
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The participants were requested to provide a written report of what they considered worth including in the published re- port. This, together with the answers of the speakers is presented in this vo- lume. I whish to thank all the speakers and discussants for their cooperativity in preparing the manuscript. The symposium was sponsored by the International Union of Biochemistry whose President, Professor Theorell, was also present and who was acting as one of the speakers and chairmen.
Opening Remarks.- Section I General.- Kinetics.- The Mechanism of Hydride Transfer.- Discussion.- The Significance of the Investigation of Model Compounds for the Elucidation of the Mechanism of Hydrogen-Transfer with Pyridine Nucleotides.- Discussion.- The Structure of Pyridine Coenzymes as Related to Binding.- Discussion.- Section II Structure and Function of Dehydrogenases.- The Primary Structure and Activity of Glyceraldehyde 3-Phosphate Dehydrogenase.- Discussion.- Quaternary Structure and Conformation of Lactic Dehydrogenase and Glyceraldehyde-3-Phosphate Dehydrogenase.- Discussion.- The Stereoselective Inhibition of Functional - SH Groups of Dehydrogenases.- Discussion.- The Role of Zinc Ions, - SH Groups, and Histidyl Residues in the Mechanism of Dehydrogenases.- Section III Alcohol and Lactate Dehydrogenases.- Structural and Functional Relationships between Isoenzymes of Horse LADH.- Discussion.- X-Ray Studies of Horse Liver Alcohol Dehydrogenase.- Discussion.- Lactate Dehydrogenase.- Discussion.- Studies on Structure and Active Sites of Lactate Dehydrogenase from Pig Heart and Pig Muscle.- Discussion.- Structure and Mechanism of Lactate Dehydrogenase.- Discussion.- Section IV Glyceraldehyde-3-Phosphate Dehydrogenases.- Selective Reactivity of Functional Groups in Glyceraldehyde 3-Phosphate Dehydrogenase.- Discussion.- On the Relationship between Protein Conformation and Enzyme-Substrate Covalent Bond Formation in Glyceraldehyde-3-Phosphate Dehydrogenase.- Discussion.- Cooperative Phenomena in Yeast Glyceraldehyde-3-Phosphate Dehydrogenase.- Discussion.- Conformational Effects of NAD+ on Yeast Glyceraldehyde-3-Phosphate Dehydrogenase.- Discussion.- Recent Studies on the Allosteric Glyceraldehyde-3-Phosphate Dehydrogenase from Yeast.- Discussion.- Subunit Interactions in Glyceraldehyde-3-Phosphate Dehydrogenase: A Fluorometric and Calorimetric Analysis of DPN Binding as a Function of Temperature.- Discussion.- Muscle Glyceraldehydephosphate Dehydrogenase: NAD+ Binding and its Implications for the Mechanism of Action of the Enzyme.- Discussion.- Section V Glutamate Dehydrogenases.- Kinetics and Mechanism of Glutamate Dehydrogenase.- Discussion.- Optical Probes for Glutamate Dehydrogenase.- Discussion.- Glutamate Dehydrogenase - A Study on its Inactivation.- Discussion.- Quaternary Structure and Enzymic Properties of Beef Liver Glutamate Dehydrogenase.- Discussion.- Structure and Association of Glutamate Dehydrogenase Solutions.- Discussion.- Mechanism of Action of Glutamate Dehydrogenase from Various Sources.- Discussion.- Section VI Different Aspects of Reactions Catalyzed by Dehydrogenases.- Kinetic Studies of NADP-Dependent Isocitrate Dehydrogenase from Beef Heart Mitochondria.- Discussion.- The Role of NAD-Linked Dehydrogenases in the Biosynthesis of UDP-D-Xylose.- Discussion.- Regulation by NADP+ and NADPH of Transhydrogenase from Azotobacter Vinelandii.- Activation Effect of 2?-Adenylic Acid on Bacterial Transhydrogenases.- Combined discussion on papers.- Section VII Pyridine Nucleotide-Dependent Flavin Enzymes.- The Role of NAD+ in the Catalytic Mechanism of Lipoamide Dehydrogenase.- Discussion.- The NADH Dehydrogenase of the Respiratory Chain.- Discussion.- A New Intermediate in TPNH-Linked Flavoproteins.- Discussion.- Section VIII Metabolic Aspects.- Regulation of the Redox State of the Pyridine Nucleotides in Rat Liver.- Discussion.- The State of the DPN System in Liver. An Analysis of Pyridine Nucleotide Levels, Surface Fluorescence, and Redox Potentials of Indicator Metabolite Couples in the Hemoglobin-Free Perfused Rat Liver.- Closing Remarks.- Index of Contributors.
Erscheint lt. Verlag | 1.1.1970 |
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Zusatzinfo | biography |
Verlagsort | Berlin |
Sprache | englisch |
Gewicht | 1100 g |
Themenwelt | Sachbuch/Ratgeber ► Gesundheit / Leben / Psychologie |
Medizin / Pharmazie ► Pflege | |
Medizin / Pharmazie ► Pharmazie ► PTA / PKA | |
ISBN-10 | 3-540-04988-6 / 3540049886 |
ISBN-13 | 978-3-540-04988-3 / 9783540049883 |
Zustand | Neuware |
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