Thiamine : catalytic mechanisms in normal and disease states /
| Other Authors: | , |
|---|---|
| Format: | Book |
| Language: | English |
| Published: |
New York :
Marcel Dekker,
[2004]
|
| Series: | Oxidative stress and disease ;
11. |
| Subjects: |
Table of Contents:
- Chemical intermediates in catalysis by thiamine diphosphate
- Mechanistic and structural studies on thiamine biosynthetic enzymes
- Studies on the structure and function of thiamine pyrophosphokinase
- New perspectives on the cellular role of thiamine triphosphate and thiamine triphosphatase
- How thiamine works in enzymes : time-resolved NMR snapshots of TDP-dependent enzymes in action
- Thiamine-dependent enzymes as catalysts of C-C bond-forming reactions : the role of "orphan" enzymes
- Ligand-induced conformational changes in thiamine diphosphate-dependent enzymes : comparison between crystal and solution structures
- Enantioselective synthesis of hydroxy ketones via benzoylformate decarboxylase- and benzaledehyde lyase-catalyzed C-C bond formation
- Benzoylformate decarboxylase : lessons in enzymology
- New concept on the nature of the induced absorption band of holotransketolase
- Structure of the α-carbanion/enamine reaction intermediate in the active site of transketolase, determined by kinetic crystallography
- Yeast pyruvate decarboxylase : new features of the structure and mechanism
- Solvent and carbon kinetic isotope effects on active-site and regulatory-site variants of yeast pyruvate decarboxylase
- Insights into the mechanism and regulation of bacterial acetohydroxyacid synthases
- Structure and properties of acetohydroxyacid synthase
- Exploring the substrate specificity of benzoylformate decarboxylase, pyruvate decarboxylase, and benzaldehyde lyase
- Benzoylformate decarboxylase : intermediates, transition states, and diversions
- Structural and functional organization of pyruvate dehydrogenase complexes
- The pyruvate dehydrogenase multienzyme complex
- Activation and transfer of lipoic acid in protein lipoylation in mammals
- Central organization of mammalian pyruvate dehydrogenase (PD) complex and lipoyl domain - mediated activated function and control of PD kinases and phosphatase 1
- Psysiological effects of replacing the PHD complex of E. coli by genetically engineered variants or by pyruvate oxidase
- Structure and intersubunit information transfer in the E. coli pyruvate dehydrogenase multienzyme complex
- Structure, function, and regulation of pyruvate dehydrogenase kinase
- Three-dimensional structures for components and domain of the mammalian branched-chain α-ketoacid dehydrogenase complex
- Variability of human pyruvate dehydrogenase complex deficiency
- Kinetic studies of human pyruvate dehydrogenase and its mutants : interaction with thiamine pyrophosphate
- The complexity of single-gene disorders : lessons from maple syrup urine disease and thiamine responsiveness
- Thiamine pyrophosphate : an essential cofactor in the mammalian metabolism of 3-methyl-branched fatty acids
- Pathogenesis of selective neuronal loss in Wernicke-Korsakoff syndrome : role of oxidative stress
- Thiamine-responsive megaloblastic anemia syndrome : clinical aspects and molecular genetics
- Accomplishments and future directions