Flavin-dependent enzymes mechanisms, structures and applications
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| Sprache: | English |
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Cambridge, MA, United States ; San Diego, CA, United States ; Kidlington, Oxford, United Kingdom ; London, United Kingdom
Academic Press, an imprint of Elsevier
2020
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| Ausgabe: | First edition |
| Schriftenreihe: | The enzymes
volume XLVII |
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| 245 | 1 | 0 | |a Flavin-dependent enzymes |b mechanisms, structures and applications |c edited by Pimchai Chaiyen, Fuyuhiko Tamanoi |
| 250 | |a First edition | ||
| 264 | 1 | |a Cambridge, MA, United States ; San Diego, CA, United States ; Kidlington, Oxford, United Kingdom ; London, United Kingdom |b Academic Press, an imprint of Elsevier |c 2020 | |
| 300 | |a 1 Online-Ressource (568 Seiten) | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b c |2 rdamedia | ||
| 338 | |b cr |2 rdacarrier | ||
| 490 | 1 | |a The enzymes |v volume XLVII | |
| 500 | |a Intro -- Flavin-Dependent Enzymes: Mechanisms, Structures and Applications -- Copyright -- Contents -- Contributors -- Preface -- Chapter One: Overview of flavin-dependent enzymes -- 1. Introduction -- 2. Flavin derivatives -- 3. Spectroscopic techniques for studying flavin chemistry -- 4. Reactions and classification of flavin-dependent enzymes -- 4.1. Flavin oxidase/dehydrogenase -- 4.2. Flavin-dependent monooxygenases -- 4.3. Flavin-dependent reductase -- 4.4. Unusual redox neutral flavin-dependent enzymes -- References -- Chapter Two: Flavoenzymes for biocatalysis -- 1. Introduction -- 2. Redox chemistry -- 2.1. Reduced flavin -- 2.1.1. CC double bond reduction -- 2.1.2. Baeyer-Villiger monooxygenation -- 2.1.3. Heteroatom oxidation -- 2.1.4. Hydroxylation -- 2.1.5. Epoxidation -- 2.2. Oxidized flavin: Dehydrogenation reactions -- 2.3. Radical catalysis via the flavin semiquinone -- 3. Addition/substitution: (De)carboxylation -- 4. Conclusions -- References -- Chapter Three: The multipurpose family of flavoprotein oxidases -- 1. Introduction -- 1.1. Flavin cofactors -- 2. Flavoprotein oxidases family -- 2.1. The VAO-type oxidase family -- 2.2. The amine oxidase family -- 2.3. The sulfhydryl oxidase family -- 2.4. The acyl-CoA oxidase-type oxidase family -- 2.5. The 2-hydroxyacid oxidase family -- 2.6. The GMC-type oxidase family -- 2.6.1. HMF oxidase -- 2.6.2. Methanol oxidase -- 3. Conclusions -- References -- Chapter Four: Vanillyl alcohol oxidase -- 1. Discovery of VAO -- 2. Initial characterization and physiological role -- 3. Substrate scope and catalytic mechanism -- 4. Crystal structure -- 5. Novel flavoprotein family -- 6. Mechanism of covalent flavinylation -- 7. Functional role of active site residues -- 8. Enzymatic synthesis of natural vanillin -- 9. The VAO/PCMH family in the post-genomic era -- References | ||
| 500 | |a Chapter Five: Porcine kidney D-amino acid oxidase-derived R-amine oxidases with new substrate specificities -- 1. Introduction -- 2. Alteration of d-amino acid oxidase from the pig kidney to R-stereoselective amine oxidase and its use in α-methylbenzy ... -- 2.1. R-stereoselective amine oxidase generation -- 2.2. Deracemization reaction with the R-stereoselective amine oxidase -- 2.3. The structure of the pkDAO variant (Y228L/R283G) -- 3. Expansion of pkDAO substrate specificity toward the S-stereoselective oxidation of 4-Cl-benzhydrylamine -- 3.1. Screening for benzhydrylamine oxidase -- 3.2. The X-ray crystallographic structure of the variant I230A/R283G complexed with (S)-4-CBHA -- 3.3. Deracemization reaction using pkDAO variant (I230A/R283G) -- 4. New enzymatic methods for primary α-aminonitrile and unnatural α-amino acid synthesis by the oxidative cyanation of pr ... -- 4.1. Screening the enzyme suitable for primary α-aminonitrile synthesis by oxidative cyanation -- 4.2. Cascade reaction for the synthesis of primary amine-derived unnatural α-amino acids -- 5. Concluding remarks -- Acknowledgments -- Conflict of interest -- References -- Chapter Six: Choline oxidases -- 1. Introduction -- 2. Physiological role -- 3. Biotechnological applications -- 4. Enzyme structure -- 5. Flavin biophysics -- 6. Steady-state kinetic mechanism -- 7. Overall turnover -- 8. Substrate gate -- 9. Substrate binding -- 10. Catalytic base -- 11. Choline alkoxide -- 12. Active site preorganization -- 13. Mechanism of alcohol oxidation -- 14. Quantum mechanical tunneling -- 15. Oxygen gate -- 16. Oxygen localization -- 17. Oxygen activation -- 18. Mechanism of oxygen reduction -- 19. Protein-flavin adducts -- 20. Incompetent forms of enzyme -- 21. Eukaryotic choline oxidase -- 22. Membrane-associated choline dehydrogenase -- 23. Conclusions -- Acknowledgments | ||
| 500 | |a References -- Chapter Seven: Reaction mechanisms and applications of aryl-alcohol oxidase -- 1. Introduction to AAO -- 1.1. AAO: A member of the GMC superfamily -- 1.2. Biological function -- 2. Structural and functional features -- 2.1. Protein structure -- 2.2. Catalytic mechanism -- 3. Biotechnological application -- 3.1. Delignification and dye decolorization -- 3.2. Deracemization of secondary alcohols -- 3.3. Production of furandicarboxylic acid -- 3.4. Flavor and fragrance production -- Acknowledgments -- References -- Chapter Eight: Structure and function relationships of sugar oxidases and their potential use in biocatalysis -- 1. Introduction -- 2. Pyranose 2-oxidase (P2O) -- 2.1. Structure and function -- 2.2. Overall catalytic reactions of P2O -- 2.2.1. Flavin reduction (sugar oxidation) mechanism -- 2.2.2. Flavin re-oxidation (oxygen reactivity) mechanism -- 2.3. Biocatalytic applications -- 2.4. Biosensor applications -- 3. Glucose oxidase (GO) -- 3.1. Structure and function -- 3.2. Overall catalytic reactions of GO -- 3.2.1. Flavin reduction (sugar oxidation) mechanism -- 3.2.2. Flavin re-oxidation (oxygen reactivity) mechanism -- 3.3. Biocatalytic applications -- 3.4. Biosensor applications -- 4. Other sugar oxidases -- 4.1. Hexose oxidase (HO) -- 4.2. Oligosaccharide oxidase -- 4.2.1. Gluco-oligosaccharide oxidase (GOOX) -- 4.2.2. Xylo-oligosaccharide oxidase (XylO) -- 4.2.3. Chito-oligosaccharide oxidase (ChitO) -- 5. Conclusion -- References -- Chapter Nine: Baeyer-Villiger monooxygenases: From protein engineering to biocatalytic applications -- 1. Introduction -- 2. Versatility of BVMOs -- 3. Protein engineering of BVMOs -- 3.1. Substrate scope and sulfoxidation activity -- 3.2. Stereo-, enantio- and regioselectivity -- 3.3. Engineering the cofactor specificity -- 3.4. Improving the stability of BVMOs -- 3.5. Promiscuity | ||
| 500 | |a 4. Biocatalytic applications of BVMOs -- 4.1. Single enzyme transformations -- 4.2. BVMOs involved in cascade reactions -- 5. Examples of preparative scale Baeyer-Villiger reactions -- 6. Conclusion and outlook -- References -- Chapter Ten: Phenolic hydroxylases -- 1. Introduction -- 2. Flavin-dependent phenolic hydroxylases -- 2.1. General reaction of single-component flavin-dependent phenolic hydroxylases -- 2.2. General reaction of two-component flavin-dependent phenolic hydroxylases -- 3. Structural basis of phenolic flavin-dependent hydroxylases -- 3.1. Single-component flavin-dependent hydroxylases -- 3.1.1. Overall structure of single-component hydroxylases -- 3.1.2. Protein dynamics during the catalysis of single-component hydroxylases -- 3.2. Two-component flavin-dependent hydroxylases -- 3.2.1. Overall structures of two-component flavin-dependent hydroxylases -- 3.2.2. Active site of C2 monooxygenase -- 4. Reaction mechanism of flavin-dependent phenolic hydroxylases -- 4.1. Unifying the catalytic features of the reaction mechanisms of phenolic flavin-dependent monooxygenases -- 4.1.1. Reaction of reduced flavin with molecular oxygen -- 4.1.2. Hydroxylation mechanism -- 4.2. Reaction mechanism of 4-hydroxybenzoate 3-hydroxylase (PHBH) -- 4.3. Reaction mechanism of 3-hydroxybenzoate 6-hydroxylase (3HB6H) -- 4.4. Reaction mechanism of 4-hydroxyphenylacetate 3-hydroxylase -- 5. Engineering of phenolic hydroxylases for biocatalysis applications -- 5.1. Engineering of 4-hydroxyphenylacetate 3-hydroxylase to expand enzyme-substrate scope -- 5.2. Engineering the p-hydroxybenzoate hydroxylase active site for gallic acid synthesis -- 5.3. Engineering of 2-hydroxybiphenyl-3-monooxygenase to change substrate reactivity and regioselectivity -- 6. Conclusions -- Acknowledgments -- References | ||
| 500 | |a Chapter Eleven: Structures, mechanisms and applications of flavin-dependent halogenases -- 1. Introduction -- 2. Structures -- 2.1. Overall structures of FDHs -- 2.2. Flavin binding site of FDHs -- 2.3. Substrate binding site of FDHs -- 3. Structures and reactions of halogenases classified according to substrates -- 3.1. Indole halogenases -- 3.2. Pyrrole halogenases -- 3.3. Phenolic halogenases -- 3.4. Aliphatic halogenases -- 3.5. Halogenase utilizes diverse substrates -- 4. Mechanisms -- 5. Improvement of the catalytic properties of FDHs using structure-guided mutagenesis -- 5.1. Substrate scope expansion -- 5.2. Site-selective mutagenesis -- 6. Applications of FDHs -- 6.1. Scale-up biocatalytic halogenation -- 6.2. Engineered biosynthetic pathway -- 6.3. Late-stage diversification of halogenated compounds -- 7. Future perspectives -- References -- Chapter Twelve: Flavin-dependent dehalogenases -- 1. Introduction -- 2. O2-dependent dehalogenation by flavin-dependent monooxygenases -- 2.1. Single-component flavin-dependent monooxygenase -- 2.1.1. Substrate scope of PcpB -- 2.1.2. Enzymatic mechanism of PcpB -- 2.2. Two-component flavin-dependent monooxygenase -- 2.2.1. Reaction and substrate scope -- 2.2.2. Reductive half-reaction (flavin reduction) catalyzed by the reductase component -- 2.2.3. Oxidative half-reaction on the oxygenase components -- 2.2.4. Quinone reduction by flavin-dependent reductase -- 2.2.5. Enzyme engineering -- 2.2.6. Novel applications of a two-component flavin-dependent monooxygenase -- 2.3. Unusual dehalogenating flavin-dependent monooxygenase -- 3. Reductive dehalogenation by flavin-dependent reductive dehalogenase -- 3.1. Cofactor and substrate scope -- 3.2. Structure arrangement of IYD -- 3.3. Reaction mechanism of iodotyrosine dehalogenase -- 3.3.1. Reductive half-reaction of IYD. | ||
| 500 | |a 3.3.2. Oxidative half-reaction of IYD. | ||
| 700 | 1 | |a Chaiyen, Pimchai |4 edt | |
| 700 | 1 | |a Tamanoi, Fuyuhiko |0 (DE-588)104165555X |4 edt | |
| 776 | 0 | 8 | |i Erscheint auch als |n Druck-Ausgabe |z 978-0-12-820137-4 |
| 830 | 0 | |a The enzymes |v volume XLVII |w (DE-604)BV040622208 |9 47 | |
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| 999 | |a oai:aleph.bib-bvb.de:BVB01-032424958 | ||
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Datensatz im Suchindex
| DE-BY-TUM_katkey | 2509315 |
|---|---|
| DE-BY-TUM_local_url | Aggregator https://ebookcentral.proquest.com/lib/munchentech/detail.action?docID=6353615 |
| _version_ | 1816714632621981696 |
| adam_txt | |
| any_adam_object | |
| any_adam_object_boolean | |
| author2 | Chaiyen, Pimchai Tamanoi, Fuyuhiko |
| author2_role | edt edt |
| author2_variant | p c pc f t ft |
| author_GND | (DE-588)104165555X |
| author_facet | Chaiyen, Pimchai Tamanoi, Fuyuhiko |
| building | Verbundindex |
| bvnumber | BV047017424 |
| classification_rvk | WD 5050 |
| classification_tum | CHE 832 |
| collection | ZDB-30-PQE |
| ctrlnum | (ZDB-30-PQE)EBC6353615 (OCoLC)1224007634 (DE-599)BVBBV047017424 |
| discipline | Biologie Chemie |
| discipline_str_mv | Biologie Chemie |
| edition | First edition |
| format | Electronic eBook |
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Introduction -- 2. Flavin derivatives -- 3. Spectroscopic techniques for studying flavin chemistry -- 4. Reactions and classification of flavin-dependent enzymes -- 4.1. Flavin oxidase/dehydrogenase -- 4.2. Flavin-dependent monooxygenases -- 4.3. Flavin-dependent reductase -- 4.4. Unusual redox neutral flavin-dependent enzymes -- References -- Chapter Two: Flavoenzymes for biocatalysis -- 1. Introduction -- 2. Redox chemistry -- 2.1. Reduced flavin -- 2.1.1. CC double bond reduction -- 2.1.2. Baeyer-Villiger monooxygenation -- 2.1.3. Heteroatom oxidation -- 2.1.4. Hydroxylation -- 2.1.5. Epoxidation -- 2.2. Oxidized flavin: Dehydrogenation reactions -- 2.3. Radical catalysis via the flavin semiquinone -- 3. Addition/substitution: (De)carboxylation -- 4. Conclusions -- References -- Chapter Three: The multipurpose family of flavoprotein oxidases -- 1. Introduction -- 1.1. Flavin cofactors -- 2. Flavoprotein oxidases family -- 2.1. The VAO-type oxidase family -- 2.2. The amine oxidase family -- 2.3. The sulfhydryl oxidase family -- 2.4. The acyl-CoA oxidase-type oxidase family -- 2.5. The 2-hydroxyacid oxidase family -- 2.6. The GMC-type oxidase family -- 2.6.1. HMF oxidase -- 2.6.2. Methanol oxidase -- 3. Conclusions -- References -- Chapter Four: Vanillyl alcohol oxidase -- 1. Discovery of VAO -- 2. Initial characterization and physiological role -- 3. Substrate scope and catalytic mechanism -- 4. Crystal structure -- 5. Novel flavoprotein family -- 6. Mechanism of covalent flavinylation -- 7. Functional role of active site residues -- 8. Enzymatic synthesis of natural vanillin -- 9. The VAO/PCMH family in the post-genomic era -- References</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">Chapter Five: Porcine kidney D-amino acid oxidase-derived R-amine oxidases with new substrate specificities -- 1. Introduction -- 2. Alteration of d-amino acid oxidase from the pig kidney to R-stereoselective amine oxidase and its use in α-methylbenzy ... -- 2.1. R-stereoselective amine oxidase generation -- 2.2. Deracemization reaction with the R-stereoselective amine oxidase -- 2.3. The structure of the pkDAO variant (Y228L/R283G) -- 3. Expansion of pkDAO substrate specificity toward the S-stereoselective oxidation of 4-Cl-benzhydrylamine -- 3.1. Screening for benzhydrylamine oxidase -- 3.2. The X-ray crystallographic structure of the variant I230A/R283G complexed with (S)-4-CBHA -- 3.3. Deracemization reaction using pkDAO variant (I230A/R283G) -- 4. New enzymatic methods for primary α-aminonitrile and unnatural α-amino acid synthesis by the oxidative cyanation of pr ... -- 4.1. Screening the enzyme suitable for primary α-aminonitrile synthesis by oxidative cyanation -- 4.2. Cascade reaction for the synthesis of primary amine-derived unnatural α-amino acids -- 5. Concluding remarks -- Acknowledgments -- Conflict of interest -- References -- Chapter Six: Choline oxidases -- 1. Introduction -- 2. Physiological role -- 3. Biotechnological applications -- 4. Enzyme structure -- 5. Flavin biophysics -- 6. Steady-state kinetic mechanism -- 7. Overall turnover -- 8. Substrate gate -- 9. Substrate binding -- 10. Catalytic base -- 11. Choline alkoxide -- 12. Active site preorganization -- 13. Mechanism of alcohol oxidation -- 14. Quantum mechanical tunneling -- 15. Oxygen gate -- 16. Oxygen localization -- 17. Oxygen activation -- 18. Mechanism of oxygen reduction -- 19. Protein-flavin adducts -- 20. Incompetent forms of enzyme -- 21. Eukaryotic choline oxidase -- 22. Membrane-associated choline dehydrogenase -- 23. Conclusions -- Acknowledgments</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">References -- Chapter Seven: Reaction mechanisms and applications of aryl-alcohol oxidase -- 1. Introduction to AAO -- 1.1. AAO: A member of the GMC superfamily -- 1.2. Biological function -- 2. Structural and functional features -- 2.1. Protein structure -- 2.2. Catalytic mechanism -- 3. Biotechnological application -- 3.1. Delignification and dye decolorization -- 3.2. Deracemization of secondary alcohols -- 3.3. Production of furandicarboxylic acid -- 3.4. Flavor and fragrance production -- Acknowledgments -- References -- Chapter Eight: Structure and function relationships of sugar oxidases and their potential use in biocatalysis -- 1. Introduction -- 2. Pyranose 2-oxidase (P2O) -- 2.1. Structure and function -- 2.2. Overall catalytic reactions of P2O -- 2.2.1. Flavin reduction (sugar oxidation) mechanism -- 2.2.2. Flavin re-oxidation (oxygen reactivity) mechanism -- 2.3. Biocatalytic applications -- 2.4. Biosensor applications -- 3. Glucose oxidase (GO) -- 3.1. Structure and function -- 3.2. Overall catalytic reactions of GO -- 3.2.1. Flavin reduction (sugar oxidation) mechanism -- 3.2.2. Flavin re-oxidation (oxygen reactivity) mechanism -- 3.3. Biocatalytic applications -- 3.4. Biosensor applications -- 4. Other sugar oxidases -- 4.1. Hexose oxidase (HO) -- 4.2. Oligosaccharide oxidase -- 4.2.1. Gluco-oligosaccharide oxidase (GOOX) -- 4.2.2. Xylo-oligosaccharide oxidase (XylO) -- 4.2.3. Chito-oligosaccharide oxidase (ChitO) -- 5. Conclusion -- References -- Chapter Nine: Baeyer-Villiger monooxygenases: From protein engineering to biocatalytic applications -- 1. Introduction -- 2. Versatility of BVMOs -- 3. Protein engineering of BVMOs -- 3.1. Substrate scope and sulfoxidation activity -- 3.2. Stereo-, enantio- and regioselectivity -- 3.3. Engineering the cofactor specificity -- 3.4. Improving the stability of BVMOs -- 3.5. Promiscuity</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">4. Biocatalytic applications of BVMOs -- 4.1. Single enzyme transformations -- 4.2. BVMOs involved in cascade reactions -- 5. Examples of preparative scale Baeyer-Villiger reactions -- 6. Conclusion and outlook -- References -- Chapter Ten: Phenolic hydroxylases -- 1. Introduction -- 2. Flavin-dependent phenolic hydroxylases -- 2.1. General reaction of single-component flavin-dependent phenolic hydroxylases -- 2.2. General reaction of two-component flavin-dependent phenolic hydroxylases -- 3. Structural basis of phenolic flavin-dependent hydroxylases -- 3.1. Single-component flavin-dependent hydroxylases -- 3.1.1. Overall structure of single-component hydroxylases -- 3.1.2. Protein dynamics during the catalysis of single-component hydroxylases -- 3.2. Two-component flavin-dependent hydroxylases -- 3.2.1. Overall structures of two-component flavin-dependent hydroxylases -- 3.2.2. Active site of C2 monooxygenase -- 4. Reaction mechanism of flavin-dependent phenolic hydroxylases -- 4.1. Unifying the catalytic features of the reaction mechanisms of phenolic flavin-dependent monooxygenases -- 4.1.1. Reaction of reduced flavin with molecular oxygen -- 4.1.2. Hydroxylation mechanism -- 4.2. Reaction mechanism of 4-hydroxybenzoate 3-hydroxylase (PHBH) -- 4.3. Reaction mechanism of 3-hydroxybenzoate 6-hydroxylase (3HB6H) -- 4.4. Reaction mechanism of 4-hydroxyphenylacetate 3-hydroxylase -- 5. Engineering of phenolic hydroxylases for biocatalysis applications -- 5.1. Engineering of 4-hydroxyphenylacetate 3-hydroxylase to expand enzyme-substrate scope -- 5.2. Engineering the p-hydroxybenzoate hydroxylase active site for gallic acid synthesis -- 5.3. Engineering of 2-hydroxybiphenyl-3-monooxygenase to change substrate reactivity and regioselectivity -- 6. Conclusions -- Acknowledgments -- References</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">Chapter Eleven: Structures, mechanisms and applications of flavin-dependent halogenases -- 1. Introduction -- 2. Structures -- 2.1. Overall structures of FDHs -- 2.2. Flavin binding site of FDHs -- 2.3. Substrate binding site of FDHs -- 3. Structures and reactions of halogenases classified according to substrates -- 3.1. Indole halogenases -- 3.2. Pyrrole halogenases -- 3.3. Phenolic halogenases -- 3.4. Aliphatic halogenases -- 3.5. Halogenase utilizes diverse substrates -- 4. Mechanisms -- 5. Improvement of the catalytic properties of FDHs using structure-guided mutagenesis -- 5.1. Substrate scope expansion -- 5.2. Site-selective mutagenesis -- 6. Applications of FDHs -- 6.1. Scale-up biocatalytic halogenation -- 6.2. Engineered biosynthetic pathway -- 6.3. Late-stage diversification of halogenated compounds -- 7. Future perspectives -- References -- Chapter Twelve: Flavin-dependent dehalogenases -- 1. Introduction -- 2. O2-dependent dehalogenation by flavin-dependent monooxygenases -- 2.1. Single-component flavin-dependent monooxygenase -- 2.1.1. Substrate scope of PcpB -- 2.1.2. Enzymatic mechanism of PcpB -- 2.2. Two-component flavin-dependent monooxygenase -- 2.2.1. Reaction and substrate scope -- 2.2.2. Reductive half-reaction (flavin reduction) catalyzed by the reductase component -- 2.2.3. Oxidative half-reaction on the oxygenase components -- 2.2.4. Quinone reduction by flavin-dependent reductase -- 2.2.5. Enzyme engineering -- 2.2.6. Novel applications of a two-component flavin-dependent monooxygenase -- 2.3. Unusual dehalogenating flavin-dependent monooxygenase -- 3. Reductive dehalogenation by flavin-dependent reductive dehalogenase -- 3.1. Cofactor and substrate scope -- 3.2. Structure arrangement of IYD -- 3.3. Reaction mechanism of iodotyrosine dehalogenase -- 3.3.1. Reductive half-reaction of IYD.</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">3.3.2. 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| id | DE-604.BV047017424 |
| illustrated | Not Illustrated |
| index_date | 2024-07-03T15:58:22Z |
| indexdate | 2024-11-25T17:57:35Z |
| institution | BVB |
| isbn | 9780128201381 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-032424958 |
| oclc_num | 1224007634 |
| open_access_boolean | |
| owner | DE-91 DE-BY-TUM |
| owner_facet | DE-91 DE-BY-TUM |
| physical | 1 Online-Ressource (568 Seiten) |
| psigel | ZDB-30-PQE ZDB-30-PQE TUM_PDA_PQE_Kauf |
| publishDate | 2020 |
| publishDateSearch | 2020 |
| publishDateSort | 2020 |
| publisher | Academic Press, an imprint of Elsevier |
| record_format | marc |
| series | The enzymes |
| series2 | The enzymes |
| spellingShingle | Flavin-dependent enzymes mechanisms, structures and applications The enzymes |
| title | Flavin-dependent enzymes mechanisms, structures and applications |
| title_auth | Flavin-dependent enzymes mechanisms, structures and applications |
| title_exact_search | Flavin-dependent enzymes mechanisms, structures and applications |
| title_exact_search_txtP | Flavin-dependent enzymes mechanisms, structures and applications |
| title_full | Flavin-dependent enzymes mechanisms, structures and applications edited by Pimchai Chaiyen, Fuyuhiko Tamanoi |
| title_fullStr | Flavin-dependent enzymes mechanisms, structures and applications edited by Pimchai Chaiyen, Fuyuhiko Tamanoi |
| title_full_unstemmed | Flavin-dependent enzymes mechanisms, structures and applications edited by Pimchai Chaiyen, Fuyuhiko Tamanoi |
| title_short | Flavin-dependent enzymes |
| title_sort | flavin dependent enzymes mechanisms structures and applications |
| title_sub | mechanisms, structures and applications |
| volume_link | (DE-604)BV040622208 |
| work_keys_str_mv | AT chaiyenpimchai flavindependentenzymesmechanismsstructuresandapplications AT tamanoifuyuhiko flavindependentenzymesmechanismsstructuresandapplications |