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140122 ||| eng |
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|a 9783034883979
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|a Iriarte, Ana J.
|e [editor]
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| 245 |
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|a Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins
|h Elektronische Ressource
|c edited by Ana J. Iriarte, Herbert M. Kagan, Marino Martinez-Carrion
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| 250 |
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|a 1st ed. 2000
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| 260 |
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|a Basel
|b Birkhäuser
|c 2000, 2000
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| 300 |
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|a XV, 377 p
|b online resource
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|a Role of Branched Chain Aminotransferase Isoenzymes in the Central Nervous System -- Modulation of Gene Expression by Vitamin B6 -- Pyridoxal 5’-phosphate, Calcium Channels -- GABA-aminotransferase, a Target for Antiepileptic Drug Therapy -- Decarboxylases, D-Amino Acid Transaminase -- Mouse Ornithine Decarboxylase: Structural Comparisons to Other PLP-Dependent Enzymes -- Structural, Mechanistic Studies of Trypanosoma brucei Ornithine Decarboxylase -- Mechanistic Analysis of Dialkylglycine Decarboxylase -- Studies on an Active Site Residue, E177, That Affects Binding of the Coenzyme in D-Amino Acid Transaminase, Mechanistic Studies on a Suicide Substrate -- Biotechnology,Applications of Emerging Technologies -- Functional Properties of Immobilized Pyridoxal 5’-phosphate-dependent Enzymes Probed by Absorption Microspectrophotometry -- Characterization of Recombinant Porcine Pyridoxal Kinase Using Surface Plasmon Resonance Biosensor Technique --
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|a Common Structural Elements in the Architecture of the Cofactor-Binding Domains in Unrelated Families of Pyridoxal-dependent Enzymes -- Mitochondrial Localization of Eukaryotic NifS-Like Proteins -- Mechanistic Studies of 8-Amino-7-Oxononanoate Synthase -- Tryptophan Synthase, Tryptophanase, Serine Transhydroxymethylase -- Structure, Function of Tryptophan Synthase -- Salt Bridging, Movalent Cation Binding Regulate Catalysis, Channeling in Tryptophan Synthase -- Equilibrium Isotope Effects: Evidence for Low-Barrier H-Bonding in Tryptophanase -- 3-Dimensional Structures of Rabbit Cytosolic, E. coli Serine Hydroxymethyltransferase -- Role of Y65, E57 in Escherichia coli Serine Hydroxymethyltransferase -- Reaction, Structure of 1-aminocyclopropane- 1 -carboxylate Deaminase -- Transaminases -- Refined Reaction Mechanism of Aspartate Aminotransferase -- 1H, 15N NMR Spectroscopy of Aspartate Aminotransferase, Related Schiff Bases, Tautomerism in Enzyme Active Sites --
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|a Structure, Induced Fit, Substrate Recognition of E. coli Branched-Chain Amino Acid Aminotransferase -- Structure, Mechanisms of Quinoenzymes -- Tryptophan Tryptophylquinone Enzymes: Structure, Function -- Continuous-Flow Column Electrolytic Spectroelectrochemical Method for Determination of Protein Redox Potentials - Application to Quinoproteins -- Enantioselectivity of PQQ-containing Alcohol Dehydrogenases: Kinetic,Thermodynamic, Molecular Modeling -- Structural Studies of a Soluble Monomeric Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5 -- Electron Transport Systems for Quinohemoprotein Type II Alcohol Dehydrogenase of Pseudomonas putida HK5 -- Cellular,Molecular Biology: Models with PLP-Dependent Proteins -- Activation,Transformation of Cells Induce Translocation of Ornithine Decarboxylase (ODC) to the Surface Membrane -- A Partially Folded Conformation Is Not the Only Requirement for Import of Mitochondrial Aspartate Aminotransferase --
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|a Engineering of B6Enzymes -- Association of Newly Synthesized Mitochondrial Aspartate Aminotransferase with Cytosolic -- Heterologous Expression, Purification of Serine Palmitoyltranferase -- Dehydratases, Lyases, Other PLP-dependent Proteins -- 5-Aminolevulinate Synthase: Pre-Steady State Reaction, Functional Role of Specific Active Site Residues -- Functional Role of PLP in Bacterial Phosphorylases -- Inhibition, Structural Changes of O-Acetylserine SulEhydrylase-A from Salmonella typhimurium upon Binding Sulfate, Chloride Anions -- Structure-Function Relationships of Porcine Pyridoxal Kinase -- The Contribution of a Conformationally-Mobile, Active-Site Loop to the Reaction Catalysed by Glutamate Semialdehyde Aminomutase -- The Reactions of Glutamate 1-Semialdehyde Aminomutase with (R), (S) Enantiomers of a Novel, Mechanism-Based Inhibitor, 2, 3-Diaminopropyl Sulfate -- Structure, Function of E. Coli Pyridoxine Phosphate Oxidase -- Molecular Pathology, Medicine --
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|a Physiological Importance of Pyrroloquinoline Quinone -- Mechanism of Topa Quinone Biogenesis in Copper Amine Oxidase Studied by Site-Directed Mutagenesis, X-ray Crystallography -- Lysyl Oxidase Activates the Transcription Activity of Collagen III Promoter: Possible Involvement of KU Antigen -- TGF-ß l Regulation of Gingival Lysyl Oxidase, Connective Tissue Growth Factor -- Pyridoxine, Dopa Decarboxylase, Tetrahydroisoquinoline Derivatives in Parkinson’s Disease -- Lysyl Oxidase -- Lysyl Oxidase: A Family of Multifunctional Proteins -- Structural Aspects of Lysyl Oxidase -- Chemotaxis of Vascular Smooth Muscle Cells by Lysyl Oxidase -- Evolution, Biological Implications -- Biological Implications of the Different Hsp70 Binding Properties of Mitochondrial, Cytosolic Aspartate Aminotransferase -- Molecular Evolution of Alanine: Glyoxylate AminotransferaseIntracellular Targeting --
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|a Three-Dimensional Model of the ATP-Binding Domain of Pyridoxal Kinase -- Structural Fluctuations of Pyridoxal Kinase: Effect of Viscogen Cosolvents -- The Aspartate Aminotransferase Folding Intermediates Recognized by GroEL are Partially Folded Monomers that Bind Pyridoxal Phosphate -- Author Index
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|a Molecular Regulation of Enzymes Controlling Levels of Vitamin B6 -- Genetic, Genomic Approaches for Delineating the Pathway of Pyridoxal 5’-Phosphate Coenzyme Biosynthesis inEscherichia coli -- Enzymes Catalysing Formation of Pyridoxal Phosphate from Vitamin B6 -- A Divergence in the Biosynthetic Pathway, a New Role for Vitamin B6 -- Molecular Cloning, Catalytic Properties of Human Brain Pyridoxal Kinase -- Regulation of Gene Expression of PLP-dependent Proteins -- Regulation of the Aspartate,Alanine Aminotransferases in Human, Rodents -- Mimosine’s Mechanism is Pyridoxal-Phosphate Independent -- Environmental Stimuli, Regulatory Factors Affecting the Expression of the Glutamic Acid Decarboxylase System in Escherichia coli -- PQQ, Quinoproteins: Biology, Regulation -- The Membrane Glucose Dehydrogenase of Escherichia coli -- Structural Properties of Homodimeric Quinoprotein Ethanol Dehydrogenase from Pseudomonas aeruginosa --
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| 653 |
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|a Cell Biology
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| 653 |
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|a Internal medicine
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| 653 |
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|a Medicine / Research
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| 653 |
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|a Protein Biochemistry
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| 653 |
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|a Cytology
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| 653 |
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|a Biology / Research
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| 653 |
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|a Internal Medicine
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| 653 |
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|a Biochemistry
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| 653 |
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|a Biomedical Research
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| 653 |
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|a Proteins
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| 700 |
1 |
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|a Kagan, Herbert M.
|e [editor]
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| 700 |
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|a Martinez-Carrion, Marino
|e [editor]
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| 041 |
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|a eng
|2 ISO 639-2
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| 989 |
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|b SBA
|a Springer Book Archives -2004
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| 028 |
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|a 10.1007/978-3-0348-8397-9
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| 856 |
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|u https://doi.org/10.1007/978-3-0348-8397-9?nosfx=y
|x Verlag
|3 Volltext
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|a 572
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| 520 |
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|a Since the first international meeting on Vitamin B6 involvement in catalysis took place in 1962, there have been periodic meetings every three or four years. In 1990, scientists studying another cofactor, PQQ, which had already attracted the scientific community's interest for its possible involvement in amino acid decarboxylation and reactions involving amino groups, joined forces with those investigating pyridoxal phosphate-dependent enzymes. Since then, the international PQQ/quinoproteins meetings have been held jointly. In the years following the original meeting 37 years ago in Rome, Italy, the scientific gatherings have taken place in Moscow, Russia (1966); Nagoya, Japan (1967); Leningrad (St. Petersburg), Russia (1974); Toronto, Canada (1979); Athens, Greece (1983); Turku, Finland (1987); Osaka, Japan (1990); and Capri, Italy (1996). For the first time in the history of these symposia, the international meeting was held in the United States, from October 31 through November 5, 1999, in Santa Fe, New Mexico. The scientific program focus shifted significantly beyond the original emphasis on catalysis to aspects such as cellular and genetic regulation of events involving proteins that require pyridoxal phosphate or quinoproteins. The growing awareness of the involvement of these proteins in biotechnology processes and fundamental physiological events, as well as their implication in diseases, was also represented, with emphasis on the molecular basis of these events. The meeting was symposium S278, sponsored by the International Union of Biochemistry and Molecular Biology (IUBMB)
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