Pyridine Nucleotide-Dependent Dehydrogenases : Proceedings of the Second International Symposium Held at the University of Konstanz, West Germany. March 28–April 1, 1977

Die seit 1925 erscheinenden Arbeiten zur Kirchengeschichte bilden eine der traditionsreichsten historischen Buchreihen im deutschsprachigen Raum. Sie enthalten Forschungen zur Kirchen- und Dogmengeschichte des Christentums aller Epochen, veröffentlichen aber auch Arbeiten aus verwandten Disziplinen wie beispielsweise der Archäologie, Kunstgeschichte oder Literaturwissenschaft. Kennzeichnend für die Reihe ist der durchgängige Anspruch, historisch-methodische Präzision mit systematischen Kontextualisierungen des jeweiligen Gegenstandes zu verbinden. In jüngerer Zeit erscheinen verstärkt Arbeiten zu Themen einer Kultur- und Ideengeschichte des Christentums in einem methodisch offenen christentumsgeschichtlichen Horizont. Opening Remarks And Deface Contents List Of Contributors Section I. Primary Structure And Conformation Conformational Adaptations Among Dehydrogenases The Primary Structures Of Chicken Lactate Dehydrogenase M 4 And H 4 Isoenzymes Structure And Properties Of Glyceraldehyde 3-Phosphate Dehydrogenase From Thermophilic Microorganisms Comparative Aspects Of Structural Studies Of Alcohol Dehydrogenases X-ray Diffraction Studies on Sheep Liver 6-Phosphogluconate Dehydrogenase at 6Å Resolution Section II. Symmetry and Coenzyme Binding Conformational Changes and Non-Equivalence in the Binding of NAD + to Cytoplasmic Malate Dehydrogenase The Effect of Nucleotide Binding on Subunit Interactions in Glyceraldehyde 3-Phosphate Dehydrogenase as Determined by the Kinetics and Thermodynamics of Subunit Exchange Dinucleotide Dependent Conformational and Chemical Bonding Changes in Muscle Glyceraldehyde-3-PO 4 Dehydrogenase Non Equivalent Active Sites in Transient Kinetics of Sturgeon Glyceraldehyde-3-Phosphate Dehydrogenase Symmetry and NAD + -Dependent Structural Changes in D-Glyceraldehyde- 3-Phosphate Dehydrogenase The Unimer Model of Glutamate Dehydrogenase: A Verification Using Chemical Modification The Immobilization Technique as an Aid in the Study of the Quaternary Structure of Dehydrogenases with Special Reference to Subunit Association and Allosteric Regulation Section III. Chemical Mechanism and Coenzyme Binding On the mode of hydrogen transfer and catalysis in nicotinamide-dependent oxidoreduction Spectrophotometric and Kinetic Identification of Transient Intermediates in the Horse Liver Alcohol Dehydrogenase Catalyzed Reduction of some Aromatic Substrates Conformation of NAD + in Solution, in Holoenzymes and in the Crystalline Li + Complex Conformation of ɛNAD + in Solution and Bound to Dehydrogenases Revealed by Fluorescence Decay Kinetics Affinity labeling by alkylating analogues of NAD Immobilized Adenine Coenzymes in General Ligand Affinity Chromatography and their Use as Active Coenzymes The Interaction of Glutamate Dehydrogenase with Ligands Thermodynamics of the LDH Reaction The Equilibrium NADH + NADP + \=\NAD + + NADPH as Studied by Transhydrogenase Section IV. Structure Function Relationship Functional Significance of the Structure of Liver Alcohol Dehydrogenase Substrate Orientation in the Active Site of Liver Alcohol Dehydrogenase Equilibrium Studies and Kinetics of Reactivation, Refolding and Reassociation of Lactic Dehydrogenase and Glyceraldehyde-3- Phosphate Dehydrogenase Studies on Dehydrogenases from Halobacterium of the Dead Sea Organization of a Bifunctional Enzyme: Escherichia Coli Aspartokinase I-Homoserine Dehydrogenase I. Relationships between the Catalytic and Regulatory Functions Chemical Probes of Topography and Subunit Interactions in a Simple Dehydrogenase and a Multienzyme Complex Section V. Kinetics and Regulation Pressure Relaxation of the Equilibrium of the Reaction Catalyzed by Pig Heart Lactate Dehydrogenase: a Test of the Kinetic Mechanism The Role of Conformational Changes in the Liver Alcohol Dehydrogenase Reaction Mechanism The Mechanism of Glutamate Dehydrogenase: Some Kinetic Aspects Regulation of Isociträte Oxidation by TPN- and DPN-Isociträte Dehydrogenases Cinnamoyl-CoA:NADPH Oxidoreductase and Cinnamyl Alcohol Dehydrogenase: two Enzymes of Lignin Monomer Biosynthesis Octopine Dehydrogenase. Spectroscopic and Conformational Properties of Bound Coenzyme, and a Possible Temperature-Regulation Function An Oil-Water-Histidine Mechanism for the Activation of Coenzyme in the a-Hydroxyacid Dehydrogenases Concluding Remarks Index of Contributors Subject Index