Title | Pyridine Nucleotide-Dependent Dehydrogenases [electronic resource] : Proceedings of an Advanced Study Institute held at the University of Konstanz, Germany, September 15-20, 1969 / edited by Horst Sund |
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Imprint | Berlin, Heidelberg : Springer Berlin Heidelberg, 1970 |
Connect to | http://dx.doi.org/10.1007/978-3-642-49974-6 |
Descript | XV, 472 p. online resource |
Opening Remarks -- Section I General -- Kinetics -- The Mechanism of Hydride Transfer -- The Significance of the Investigation of Model Compounds for the Elucidation of the Mechanism of Hydrogen-Transfer with Pyridine Nucleotides -- The Structure of Pyridine Coenzymes as Related to Binding -- Section II Structure and Function of Dehydrogenases -- The Primary Structure and Activity of Glyceraldehyde 3-Phosphate Dehydrogenase -- Quaternary Structure and Conformation of Lactic Dehydrogenase and Glyceraldehyde-3-Phosphate Dehydrogenase -- The Stereoselective Inhibition of Functional โ SH Groups of Dehydrogenases -- The Role of Zinc Ions, โ 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 -- X-Ray Studies of Horse Liver Alcohol Dehydrogenase -- Lactate Dehydrogenase -- Studies on Structure and Active Sites of Lactate Dehydrogenase from Pig Heart and Pig Muscle -- Structure and Mechanism of Lactate Dehydrogenase -- Section IV Glyceraldehyde-3-Phosphate Dehydrogenases -- Selective Reactivity of Functional Groups in Glyceraldehyde 3-Phosphate Dehydrogenase -- On the Relationship between Protein Conformation and Enzyme-Substrate Covalent Bond Formation in Glyceraldehyde-3-Phosphate Dehydrogenase -- Cooperative Phenomena in Yeast Glyceraldehyde-3-Phosphate Dehydrogenase -- Conformational Effects of NAD+ on Yeast Glyceraldehyde-3-Phosphate Dehydrogenase -- Recent Studies on the Allosteric Glyceraldehyde-3-Phosphate Dehydrogenase from Yeast -- Subunit Interactions in Glyceraldehyde-3-Phosphate Dehydrogenase: A Fluorometric and Calorimetric Analysis of DPN Binding as a Function of Temperature -- Muscle Glyceraldehydephosphate Dehydrogenase: NAD+ Binding and its Implications for the Mechanism of Action of the Enzyme -- Section V Glutamate Dehydrogenases -- Kinetics and Mechanism of Glutamate Dehydrogenase -- Optical Probes for Glutamate Dehydrogenase -- Glutamate Dehydrogenase โ A Study on its Inactivation -- Quaternary Structure and Enzymic Properties of Beef Liver Glutamate Dehydrogenase -- Structure and Association of Glutamate Dehydrogenase Solutions -- Mechanism of Action of Glutamate Dehydrogenase from Various Sources -- Section VI Different Aspects of Reactions Catalyzed by Dehydrogenases -- Kinetic Studies of NADP-Dependent Isocitrate Dehydrogenase from Beef Heart Mitochondria -- The Role of NAD-Linked Dehydrogenases in the Biosynthesis of UDP-D-Xylose -- Regulation by NADP+ and NADPH of Transhydrogenase from Azotobacter Vinelandii -- Activation Effect of 2?-Adenylic Acid on Bacterial Transhydrogenases -- Section VII Pyridine Nucleotide-Dependent Flavin Enzymes -- The Role of NAD+ in the Catalytic Mechanism of Lipoamide Dehydrogenase -- The NADH Dehydrogenase of the Respiratory Chain -- A New Intermediate in TPNH-Linked Flavoproteins -- Section VIII Metabolic Aspects -- Regulation of the Redox State of the Pyridine Nucleotides in Rat Liver -- 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