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Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems.
The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. Thisfirst book of thetwo volume set provides an overview of all aspects focussing on oxidases, dehydrogenases and related systems. Discussed arerecent developments in this field including those of l...
| Clasificación: | Libro Electrónico |
|---|---|
| Autor principal: | |
| Otros Autores: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Berlin :
De Gruyter,
2012.
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| Colección: | Handbook of Flavoproteins ;
Volume 1 |
| Temas: | |
| Acceso en línea: | Texto completo |
Tabla de Contenidos:
- Preface; 1 Berberine bridge enzyme and the family of bicovalent flavoenzymes; 1.1 Introduction; 1.2 The paradigm of bicovalent flavoenzymes: Berberine bridge enzyme (BBE) from Eschscholzia californica; 1.3 The family of BBE-like enzymes in the plant kingdom: how many and what for?; 1.4 The occurrence of BBE-like enzymes in fungi; 1.5 BBE-like enzymes in bacteria: oxidative power for the biosynthesis of antibiotics; 1.6 Conclusions; 1.7 Acknowledgments; 1.8 References; 2 PutA and proline metabolism; 2.1 Importance of proline metabolism; 2.2 Proline utilization A (PutA) proteins.
- 2.3 Three-dimensional structures of PutA and PutA domains2.3.1 Structures of the catalytic domains of PutA; 2.3.2 Crystal structure of a minimalist PutA; 2.3.3 Solution structure of a trifunctional PutA and the role of the CTD; 2.4 Reaction kinetics of PutA; 2.4.1 Proline:ubiquinone oxidoreductase activity; 2.4.2 Substrate channeling; 2.5 DNA and membrane binding of trifunctional PutA; 2.5.1 DNA binding; 2.5.2 Membrane association; 2.6 PutA functional switching; 2.6.1 Redox-linked global conformational changes; 2.6.2 Local structural changes near the flavin.
- 2.6.3 Residues important for functional switching2.7 Conclusions and future research directions; 2.8 Acknowledgements; 2.9 References; 3 Flavoenzymes involved in non-redox reactions; 3.1 Introduction; 3.2 Flavoenzymes for which flavin cofactors likely play redox-based catalytic roles; 3.2.1 Chorismate synthase; 3.2.2 4-Hydroxybutyryl-CoA dehydratase; 3.2.3 Polyunsaturated fatty acid isomerase; 3.2.4 4'-Phosphopantothenoylcysteine decarboxylase; 3.2.5 Other examples; 3.3 Flavoenzymes for which flavin cofactors likely play non-redox catalytic roles.
- 3.3.1 Type 2 isopentenyl diphosphate isomerase3.3.2 UDP-galactopyranose mutase; 3.4 Flavoenzymes for which flavin cofactors play uncertain, but probably catalytic roles; 3.4.1 Lycopene cyclase; 3.4.2 Carotene cis-trans isomerase; 3.4.3 Fatty acid hydratase; 3.4.4 2-Haloacrylate hydratase; 3.5 Conclusions; 3.6 References; 4 Enzymes of FMN and FAD Metabolism; 4.1 Introduction; 4.2 Enzymes involved in the production of FMN and FAD in different organisms; 4.3 FMN and FAD metabolism in yeasts and mammals; 4.4 FMN and FAD metabolism in bacteria depends on a bifunctional enzyme.
- 4.5 FMN and FAD metabolism in plants4.6 Conclusions and future research directions; 4.7 Acknowledgments; 4.8 References; 4.9 Abbreviations; 5 Mechanisms of bacterial luciferase and related flavin reductases; 5.1 Introduction; 5.2 Luciferase mechanism overview; 5.2.1 Mechanism of chemiexcitation; 5.2.2 Identity of primary excited state and emitter; 5.2.3 Multiple forms of 4a-hydroperoxy-FMNH intermediate II; 5.2.4 Aldehyde substrate inhibition; 5.3 Flavin reductases
- general remarks; 5.3.1 Mechanisms of flavin reductases in single-enzyme reactions.