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...
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| 1. Verfasser: | |
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| Weitere Verfasser: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Berlin :
De Gruyter,
2012.
|
| Schriftenreihe: | Handbook of Flavoproteins ;
Volume 1 |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Zusammenfassung: | 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 large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes. |
| Beschreibung: | 5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions. |
| Beschreibung: | 1 online resource (372 pages) |
| Bibliographie: | Includes bibliographical references and index. |
| ISBN: | 9783110268911 3110268914 |
Internformat
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| 260 | |a Berlin : |b De Gruyter, |c 2012. | ||
| 300 | |a 1 online resource (372 pages) | ||
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| 505 | 0 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 500 | |a 5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions. | ||
| 520 | |a 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 large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes. | ||
| 504 | |a Includes bibliographical references and index. | ||
| 546 | |a In English. | ||
| 650 | 0 | |a Flavoproteins. |0 http://id.loc.gov/authorities/subjects/sh85049033 | |
| 650 | 6 | |a Flavoprotéines. | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Flavoproteins |2 fast | |
| 700 | 1 | |a Gregersen, Niels Henrik, |d 1956- |1 https://id.oclc.org/worldcat/entity/E39PBJcRfpFRy8Wm7pMWbHtqcP |0 http://id.loc.gov/authorities/names/n90677524 | |
| 700 | 1 | |a Rokita, Steven Edward. |0 http://id.loc.gov/authorities/names/n88624564 | |
| 700 | 1 | |a Becker, Donald. |0 http://id.loc.gov/authorities/names/nb2008012535 | |
| 700 | 1 | |a Hille, Russ. |0 http://id.loc.gov/authorities/names/n2012189060 | |
| 700 | 1 | |a Palfey, Bruce. |0 http://id.loc.gov/authorities/names/n2012189061 | |
| 700 | 1 | |a Binda, Claudia. | |
| 700 | 1 | |a Ceccarelli, Eduardo. | |
| 700 | 1 | |a Chaiyen, Pimchai. | |
| 700 | 1 | |a Costa Filho, Antonio J. | |
| 700 | 1 | |a Daniel, Bastian. | |
| 700 | 1 | |a Dully, Corinna. | |
| 700 | 1 | |a Edmondson, D. E. |0 http://id.loc.gov/authorities/names/n82121723 | |
| 700 | 1 | |a Fitzpatrick, Paul. | |
| 700 | 1 | |a Gadda, Giovanni. | |
| 700 | 1 | |a Ghisla, S. |q (Sandro), |d 1942- |1 https://id.oclc.org/worldcat/entity/E39PCjthGXvFtfKhqhFR3bRKcX |0 http://id.loc.gov/authorities/names/n89123992 | |
| 700 | 1 | |a Hemmi, Hisashi. | |
| 700 | 1 | |a Jentoft Olsen, Rikke Katrine. | |
| 700 | 1 | |a Kim, Jung-Ja. | |
| 700 | 1 | |a Macheroux, Peter. | |
| 700 | 1 | |a Mattevi, Andrea. | |
| 700 | 1 | |a Medina, M. |q (Milagros) |1 https://id.oclc.org/worldcat/entity/E39PCjJRCHXmR4C3K47WjKDdcd |0 http://id.loc.gov/authorities/names/n2010180025 | |
| 700 | 1 | |a Nonato, Maria Cristina. | |
| 700 | 1 | |a Schuman Jorns, Marilyn. | |
| 700 | 1 | |a Tanner, John J. | |
| 700 | 1 | |a Thorpe, Colin. | |
| 700 | 1 | |a Tu, Shiao-Chun. | |
| 700 | 1 | |a Vanoni, Maria A. | |
| 700 | 1 | |a Wallner, Silvia. | |
| 700 | 1 | |a Wongnate, Thanyaporn. | |
| 758 | |i has work: |a Handbook of flavoproteins (Text) |1 https://id.oclc.org/worldcat/entity/E39PCGF4rjwQJY7dQcJg4XHwG3 |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |a Miller, Susan. |t Handbook of Flavoproteins : Volume 1 Oxidases, Dehydrogenases and Related Systems. |d Berlin : De Gruyter, ©2012 |z 9783110268423 |
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| author | Miller, Susan, 1955 December 21- |
| author2 | Gregersen, Niels Henrik, 1956- Rokita, Steven Edward Becker, Donald Hille, Russ Palfey, Bruce Binda, Claudia Ceccarelli, Eduardo Chaiyen, Pimchai Costa Filho, Antonio J. Daniel, Bastian Dully, Corinna Edmondson, D. E. Fitzpatrick, Paul Gadda, Giovanni Ghisla, S. (Sandro), 1942- Hemmi, Hisashi Jentoft Olsen, Rikke Katrine Kim, Jung-Ja Macheroux, Peter Mattevi, Andrea Medina, M. (Milagros) Nonato, Maria Cristina Schuman Jorns, Marilyn Tanner, John J. Thorpe, Colin Tu, Shiao-Chun Vanoni, Maria A. Wallner, Silvia Wongnate, Thanyaporn |
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| author_facet | Miller, Susan, 1955 December 21- Gregersen, Niels Henrik, 1956- Rokita, Steven Edward Becker, Donald Hille, Russ Palfey, Bruce Binda, Claudia Ceccarelli, Eduardo Chaiyen, Pimchai Costa Filho, Antonio J. Daniel, Bastian Dully, Corinna Edmondson, D. E. Fitzpatrick, Paul Gadda, Giovanni Ghisla, S. (Sandro), 1942- Hemmi, Hisashi Jentoft Olsen, Rikke Katrine Kim, Jung-Ja Macheroux, Peter Mattevi, Andrea Medina, M. (Milagros) Nonato, Maria Cristina Schuman Jorns, Marilyn Tanner, John J. Thorpe, Colin Tu, Shiao-Chun Vanoni, Maria A. Wallner, Silvia Wongnate, Thanyaporn |
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| contents | 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. |
| ctrlnum | (OCoLC)829462145 |
| dewey-full | 572.791 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
| dewey-raw | 572.791 |
| dewey-search | 572.791 |
| dewey-sort | 3572.791 |
| dewey-tens | 570 - Biology |
| discipline | Biologie |
| format | Electronic eBook |
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;</subfield><subfield code="v">Volume 1</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Print version record.</subfield></datafield><datafield tag="505" ind1="0" ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">2.3 Three-dimensional structures of PutA and PutA domains2.3.1 Structures of the catalytic domains of PutA; 2.3.2 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examples; 3.3 Flavoenzymes for which flavin cofactors likely play non-redox catalytic roles.</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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 large membrane-integral electron transfer complexes. 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E.</subfield><subfield code="0">http://id.loc.gov/authorities/names/n82121723</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Fitzpatrick, Paul.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gadda, Giovanni.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ghisla, S.</subfield><subfield code="q">(Sandro),</subfield><subfield code="d">1942-</subfield><subfield code="1">https://id.oclc.org/worldcat/entity/E39PCjthGXvFtfKhqhFR3bRKcX</subfield><subfield code="0">http://id.loc.gov/authorities/names/n89123992</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hemmi, Hisashi.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jentoft Olsen, Rikke Katrine.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, Jung-Ja.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Macheroux, Peter.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mattevi, Andrea.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Medina, M.</subfield><subfield code="q">(Milagros)</subfield><subfield code="1">https://id.oclc.org/worldcat/entity/E39PCjJRCHXmR4C3K47WjKDdcd</subfield><subfield code="0">http://id.loc.gov/authorities/names/n2010180025</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Nonato, Maria Cristina.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Schuman Jorns, Marilyn.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tanner, John J.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Thorpe, Colin.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tu, Shiao-Chun.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Vanoni, Maria A.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wallner, Silvia.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wongnate, Thanyaporn.</subfield></datafield><datafield tag="758" ind1=" " ind2=" "><subfield code="i">has work:</subfield><subfield code="a">Handbook of flavoproteins (Text)</subfield><subfield code="1">https://id.oclc.org/worldcat/entity/E39PCGF4rjwQJY7dQcJg4XHwG3</subfield><subfield code="4">https://id.oclc.org/worldcat/ontology/hasWork</subfield></datafield><datafield tag="776" ind1="0" ind2="8"><subfield code="i">Print version:</subfield><subfield code="a">Miller, Susan.</subfield><subfield code="t">Handbook of Flavoproteins : Volume 1 Oxidases, Dehydrogenases and Related Systems.</subfield><subfield code="d">Berlin : De Gruyter, ©2012</subfield><subfield code="z">9783110268423</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="l">FWS01</subfield><subfield code="p">ZDB-4-EBA</subfield><subfield code="q">FWS_PDA_EBA</subfield><subfield code="u">https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=543960</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="938" ind1=" " ind2=" "><subfield code="a">De Gruyter</subfield><subfield code="b">DEGR</subfield><subfield code="n">9783110268911</subfield></datafield><datafield tag="938" ind1=" " ind2=" "><subfield code="a">EBL - Ebook Library</subfield><subfield code="b">EBLB</subfield><subfield code="n">EBL912850</subfield></datafield><datafield tag="938" ind1=" " ind2=" "><subfield code="a">ebrary</subfield><subfield code="b">EBRY</subfield><subfield code="n">ebr10661411</subfield></datafield><datafield tag="938" ind1=" " ind2=" "><subfield code="a">EBSCOhost</subfield><subfield code="b">EBSC</subfield><subfield code="n">543960</subfield></datafield><datafield tag="938" ind1=" " ind2=" "><subfield code="a">YBP Library Services</subfield><subfield code="b">YANK</subfield><subfield code="n">10227886</subfield></datafield><datafield tag="994" ind1=" " ind2=" "><subfield code="a">92</subfield><subfield code="b">GEBAY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-4-EBA</subfield></datafield><datafield tag="049" ind1=" " ind2=" "><subfield code="a">DE-863</subfield></datafield></record></collection> |
| id | ZDB-4-EBA-ocn829462145 |
| illustrated | Not Illustrated |
| indexdate | 2024-11-27T13:25:13Z |
| institution | BVB |
| isbn | 9783110268911 3110268914 |
| language | English |
| oclc_num | 829462145 |
| open_access_boolean | |
| owner | MAIN DE-863 DE-BY-FWS |
| owner_facet | MAIN DE-863 DE-BY-FWS |
| physical | 1 online resource (372 pages) |
| psigel | ZDB-4-EBA |
| publishDate | 2012 |
| publishDateSearch | 2012 |
| publishDateSort | 2012 |
| publisher | De Gruyter, |
| record_format | marc |
| series2 | Handbook of Flavoproteins ; |
| spelling | Miller, Susan, 1955 December 21- https://id.oclc.org/worldcat/entity/E39PCjwfrthrfxB9MQq9BKmQmb http://id.loc.gov/authorities/names/n2012189083 Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. Berlin : De Gruyter, 2012. 1 online resource (372 pages) text txt rdacontent computer c rdamedia online resource cr rdacarrier Handbook of Flavoproteins ; Volume 1 Print version record. 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. 5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions. 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 large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes. Includes bibliographical references and index. In English. Flavoproteins. http://id.loc.gov/authorities/subjects/sh85049033 Flavoprotéines. SCIENCE Life Sciences Biochemistry. bisacsh Flavoproteins fast Gregersen, Niels Henrik, 1956- https://id.oclc.org/worldcat/entity/E39PBJcRfpFRy8Wm7pMWbHtqcP http://id.loc.gov/authorities/names/n90677524 Rokita, Steven Edward. http://id.loc.gov/authorities/names/n88624564 Becker, Donald. http://id.loc.gov/authorities/names/nb2008012535 Hille, Russ. http://id.loc.gov/authorities/names/n2012189060 Palfey, Bruce. http://id.loc.gov/authorities/names/n2012189061 Binda, Claudia. Ceccarelli, Eduardo. Chaiyen, Pimchai. Costa Filho, Antonio J. Daniel, Bastian. Dully, Corinna. Edmondson, D. E. http://id.loc.gov/authorities/names/n82121723 Fitzpatrick, Paul. Gadda, Giovanni. Ghisla, S. (Sandro), 1942- https://id.oclc.org/worldcat/entity/E39PCjthGXvFtfKhqhFR3bRKcX http://id.loc.gov/authorities/names/n89123992 Hemmi, Hisashi. Jentoft Olsen, Rikke Katrine. Kim, Jung-Ja. Macheroux, Peter. Mattevi, Andrea. Medina, M. (Milagros) https://id.oclc.org/worldcat/entity/E39PCjJRCHXmR4C3K47WjKDdcd http://id.loc.gov/authorities/names/n2010180025 Nonato, Maria Cristina. Schuman Jorns, Marilyn. Tanner, John J. Thorpe, Colin. Tu, Shiao-Chun. Vanoni, Maria A. Wallner, Silvia. Wongnate, Thanyaporn. has work: Handbook of flavoproteins (Text) https://id.oclc.org/worldcat/entity/E39PCGF4rjwQJY7dQcJg4XHwG3 https://id.oclc.org/worldcat/ontology/hasWork Print version: Miller, Susan. Handbook of Flavoproteins : Volume 1 Oxidases, Dehydrogenases and Related Systems. Berlin : De Gruyter, ©2012 9783110268423 FWS01 ZDB-4-EBA FWS_PDA_EBA https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=543960 Volltext |
| spellingShingle | Miller, Susan, 1955 December 21- Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. 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. Flavoproteins. http://id.loc.gov/authorities/subjects/sh85049033 Flavoprotéines. SCIENCE Life Sciences Biochemistry. bisacsh Flavoproteins fast |
| subject_GND | http://id.loc.gov/authorities/subjects/sh85049033 |
| title | Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. |
| title_auth | Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. |
| title_exact_search | Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. |
| title_full | Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. |
| title_fullStr | Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. |
| title_full_unstemmed | Handbook of flavoproteins : Volume 1 oxidases, dehydrogenases and related systems. |
| title_short | Handbook of flavoproteins : |
| title_sort | handbook of flavoproteins volume 1 oxidases dehydrogenases and related systems |
| title_sub | Volume 1 oxidases, dehydrogenases and related systems. |
| topic | Flavoproteins. http://id.loc.gov/authorities/subjects/sh85049033 Flavoprotéines. SCIENCE Life Sciences Biochemistry. bisacsh Flavoproteins fast |
| topic_facet | Flavoproteins. Flavoprotéines. SCIENCE Life Sciences Biochemistry. Flavoproteins |
| url | https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=543960 |
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