Pyridine Nucleotide-Dependent Dehydrogenases : : Proceedings of the second International Symposium held at the University of Konstanz, West Germany. March 28–April 1, 1977 / / ed. by Horst Sund.

• Superior document: Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences - <1990
• MitwirkendeR: Adams, M.J.,; Andersson, L.,; Archibald, I.G.,; Au, A.M.-J.,; Baici, A.,; Banaszak, L.J.,; Becker, Dagobert,; Bernhard, Sidney,; Biellmann, J.F.,; Biesecker, G.,; Birktoft, J.J.,; Blankenhorn, Gunter,; Bohn, A.,; Branlant, G.,; Brändén, Carl-Ivar,; Coates, J. H.,; Dieter, H.,; Dunn, M.F.,; Dutler, Hans,; Eisenberg, H.,; Eventoff, William,; Fontan, Elisabeth,; Foucaud, B.Y.,; Gafni, A.,; Garavito, R. Michael,; Grisebach, H.,; Gutfreund, H.,; Halvorson, Herbert R.,; Hardman, M. J.,; Harris, J. Ieuan,; Helliwell, J.R.,; Hinz, Hans-Jürgen,; Holbrook, J. John,; Hollaway, M.R.,; Jaenicke, Rainer,; Jeck, R.,; Joppich-Kuhn, R.,; Jörnvall, Hans,; Kellershohn, N.,; Koberstein, R.,; Koerber, S.C.,; Krul, J.,; Leicht, W.,; Lucast, Karen D.,; Luisi, P.L.,; Malhotra, Om P.,; Markau, K.,; Mevarech, M.,; Morris, R.G.,; Mosbach, K.,; Mühlegger, K.,; Olomucki, A.,; Osborne, H.H.,; Parker, David M.,; Peetz, D.,; Perham, Richard N.,; Pfenninger, Oswald,; Plaut, Gerhard W.E.,; Rasched, I.,; Reddy, B.S.,; Rossmann, Michael G.,; Rudolph, Rainer,; Saenger, W.,; Saliman, G.,; Schack, P.,; Schmid, Franz,; Schwarzwälder, Johanna,; Schwendimann, Bernard,; Seydoux, F.J.,; Shore, Joseph D.,; Smith, Colleen M.,; Spotorno, G.M.L.,; Sund, H.,; Thomé-Beau, F.,; Torff, Hans-Joachim,; Truffa-Bachi, Paolo,; Veeger, C.,; Veeger, Cees,; Walker, John E.,; Wallén, L.,; Weber, K.,; Weimann, G.,; Weininger, M.,; Wengenmayer, H.,; Werber, M.M.,; Woenckhaus, C.,; Wonacott, A.J.,; Wyrambik, D.,
• HerausgeberIn: Sund, Horst,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2019]; ©1977
• Year of Publication: 2019
• Edition: Reprint 2019
• Language: English
• Physical Description: 1 online resource (513 p.) :; Num. figs. and tabs.

Table of Contents

• Frontmatter
• 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 M4 And H4 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-PO4 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
• Backmatter