Biochemistry of Vitamin B6: Proceedings of the 7th International Congress on Chemical and Biological

Prologue in Honour of Alexander E. Braunstein 1902-1986.- The Discovery of Enzymatic Transamination and Its Biological Significance.- Professor Alexander E. Braunstein; Some Reminiscences.- Closing Remarks.- Molecular Biology and Site-Directed Mutagenesis.- Genes, Biosynthesis, and Intracellular Processing of the Isoenzymes of Aspartate Aminotransferase.- Structure-Function Relation of the Presequence of a Precursor to Pig Mitochondrial Aspartate Aminotransferase.- Molecular Cloning and in vivo Expression of the Precursor to Rat Mitochondrial Aspartate Aminotransferase.- Rat Cytosolic Aspartate Aminotransferase; Molecular Cloning of cDNA and Expression in E. coli.- D-Amino Acid Aminotransferase from a Thermophile, Bacillus sp. YM-1: Enzymological Properties, Cloning of the Gene, and the Amino Acid Sequence.- The Subunit Structure of Porcine Ornithine Aminotransferase and Mechanism of Proteolytic Modification of Its Putative Precursors in Mitochondria.- Hepatic Systems Degrade Tyrosine Aminotransferase.- Demonstration of Immunochemical Cross-Reactivity of Dopa Decarboxylase and Histidine Decarboxylase Using Antibodies against the Two Enzymes.- Mechanistic Analysis of the Aspartate Aminotransferase Active Site Mutants - Y70F, K258A, and R292D.- Mutation of Lysine 258 to Arginine in the Active Site of Aspartate Aminotransferase.- Bacterial Tryptophan Synthetase: A Multienzyme Complex Which Contains Pyridoxal Phosphate.- Site-specific Mutations in E. coli Maltodextrin Phosphorylase with Differential Effects on Substrate Binding and Catalysis.- Aminotransferases.- Spatial Aspects of Catalysis by Mitochondrial Aspartate Aminotransferase.- Recent Studies on Mitochondrial Aspartate Aminotransferase: Structure and Mechanism.- X-Ray Crystallographic, 19F-NMR and UV-Visible Spectroscopic Studies of Pig Heart Cytosolic Aspartate Aminotransferase.- Studies of the Inactivated Coenzyme in the Beta Sub form of Cytosolic Aspartate Aminotransferase.- Studies on the Mechanism of Action of Aspartate Aminotransferase by Cryoenzymological and Isotope Techniques.- Aspartate Aminotransferase from the Thermoacidophile Archaebacterium Sulfolobus solfataricus.- Coenzyme Reorientations in the Active Sites of Aspartate Aminotransferase Isoenzymes.- Phosphorus-31 Nuclear Magnetic Resonance Studies on Apoaspartate Aminotransferase Reconstituted with Cofactor Analogues.- Fourier Transform Infrared Spectroscopic Analysis of Phosphate Bound to the Aspartate Aminotransferase Isoenzymes.- Carboxylate Inhibition of Apoaspartate Aminotransferase.- The Reversible Oxidation of Vicinal SH Groups in 4-Aminobutyrate Aminotransferase. Probes of Conformational Changes.- Branched-Chain Amino Acid Aminotransferase from Escherichia coli.- Crystallographic and Solution Studies on Phosphoserine Aminotransferase (PSAT) from E. coli.- Studies on Liver GABA-Transaminase.- A Novel Aminotransferase Concerned with the Metabolism of Dimethylarginines in Rats.- Other Vitamin B6-Enzymes of Amino Acid Metabolism.- Chemical Probes of Substrate Channeling in the E. coli Tryptophan Synthase ?2?2 Bienzyme Complex.- Phosphorus-31 NMR Study of Pyridoxal 5?-Phosphate Binding to Escherichia coli Tryptophan Synthase Modified by Limited Proteolysis.- Glutamate Decarboxylase: Preliminary Crystallographic Data.- Analysis of the Glutamate Decarboxylase Reaction by Membrane Inlet Mass Spectrometry.- Proteolytic Cleavage of Pig Kidney Dopa Decarboxylase.- The Reaction of Dopa Decarboxylase with 5?-Hydroxytryptophan Isomers.- Sequence Studies on Vitamin B6-Dependent Enzymes: Serine Hydroxymethyltransferase and Glutamate Decarboxylase.- Stereochemistry of the Threonine Cleavage Complex.- The Substrate Specificity of Tyrosine Phenol-Lyase During the Different Stages of Enzymatic Process.- Structural and Catalytic Properties of Citrobacter intermedius Tyrosine Phenol-Lyase.- L-Methionine Y-Lyase: Its Essential Cysteine Residues.- Diaminopropionate Ammonia-Lyase of Salmonella typhimurium.- Interaction