Dunming Zhu
Chemo-Enzymatic Cascade Reactions
Dunming Zhu
Chemo-Enzymatic Cascade Reactions
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Explores biocatalytic-chemical cascade reactions and their applications in the synthesis of valuable chemicals.
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Explores biocatalytic-chemical cascade reactions and their applications in the synthesis of valuable chemicals.
Hinweis: Dieser Artikel kann nur an eine deutsche Lieferadresse ausgeliefert werden.
Hinweis: Dieser Artikel kann nur an eine deutsche Lieferadresse ausgeliefert werden.
Produktdetails
- Produktdetails
- Verlag: Wiley-VCH
- Artikelnr. des Verlages: 1134451 000
- 1. Auflage
- Seitenzahl: 402
- Erscheinungstermin: 28. April 2021
- Englisch
- Abmessung: 250mm x 175mm x 26mm
- Gewicht: 898g
- ISBN-13: 9783527344512
- ISBN-10: 3527344519
- Artikelnr.: 60397882
- Verlag: Wiley-VCH
- Artikelnr. des Verlages: 1134451 000
- 1. Auflage
- Seitenzahl: 402
- Erscheinungstermin: 28. April 2021
- Englisch
- Abmessung: 250mm x 175mm x 26mm
- Gewicht: 898g
- ISBN-13: 9783527344512
- ISBN-10: 3527344519
- Artikelnr.: 60397882
Dunming Zhu, Ph.D., is a "Hundred Talents Program" Professor at Tianjin Institute of Industrial Biotechnology (TIB), Chinese Academy of Sciences (CAS), and Director of National Engineering Laboratory for Industrial Enzymes. He has been named "Thousand Talents Program" Expert by Tianjin municipal government. Prof. Zhu got his BS from the University of Science & Technology of China and his Ph.D. from Shanghai Institute of Organic Chemistry, CAS. Before joining TIB, he held several positions in academia and industry in the United States. He has co-authored more than 100 peer-reviewed articles in core international journals including JACS, ACS catalysis, Organic Letters and Advanced Synthesis & Catalysis. He has been invited to contribute several book chapters and to give talks at several international conferences including Gordon Research Conference Green Chemistry and ECI Enzyme Engineering Conference. He received a First Class Award in Natural Science by the CAS in 1995, a Third Class Award in Natural Science by the Chinese National Committee of Science and Technology in 1997, the Tetrahedron: Asymmetry Most Cited Paper 2004-2007 Award and 2005-2008 Award by Elsevier Ltd. and Outstanding Contribution Award in Collaboration with Industry by TIB in 2010. He is an Editorial Board Member of Journal of Molecular Catalysis B: Enzymatic, and ad hoc reviewer of more than 20 international journals. His research interest ranges from discovery of novel industrial enzymes to understanding of biocatalytic reaction mechanisms, and the integration of biocatalysis into complex organic synthesis.
1 Introduction
1.1 Advantages of Enzyme Catalysis
1.1.1 Chemo-selectivity
1.1.2 Regioselectivity
1.1.3 Stereoselectivity
1.1.4 Mild Reaction Conditions
1.2 Modes of Chemo-enzymatic transformations
1.2.1 "separate-pot-two-step" mode
1.2.2 "one-pot-two-step" mode
1.2.3 "one-pot-one-step" mode
1.3 Summary and outlooks
2 "Separate-Pot Two-Step" Chemo-Enzymatic Transformation
2.1 Lipases
2.2 Nitrilases
2.3 Carbonyl reductases
2.4 Ene reductases
2.5. Transaminases
2.6 Imine reductases
2.7 Cytochromes P450s
2.8 Baeyer-Villiger monooxygenases (BVMOs)
2.9 Aldolases
2.10 Epoxide hydrolases
2.11 Other Enzymes
2.12 Integration of Multi-Enzyme Cascade with Chemical Transformation
2.13 Summary and outlooks
3. One-Pot Sequential Chemoenzymatic Reactions
3.1 Lipases and Esterases
3.2 Carbonyl Reductases
3.3 Ene Reductases
3.4 Transaminases
3.5 Epoxide hydrolases (EHs)
3. 6 Other Enzymes
3.6.1 Aldolases
3.6.2 Halohydrin Dehalogenases
3.6.3 Phenylalanine Ammonia Lyases
3.6.4 D-amino Acid Dehydrogenases (DAADHs)
3.6.5 Halogenases
3.6.6 Imine Reductases
3.6.7 Decarboxylases
3.6.8 Cytochrome P450s
3.6.9 Hydroxynitrile Lyases
3.6.10 Nitrilases
3.6.11 Laccases
3.6.12 Transglutaminases
3.6.13 a-Ketoglutarate-Dependent (a-KG) non-Heme Iron Oxygenases
3.6.14 Galactose Oxidases
3.6.15 FAD-Dependent Monooxygenases
3.7 Summary and outlooks
4. Chemoenzymatic Dynamic Kinetic Resolution
4.1 Enzymatic Kinetic Resolution
4.2 Dynamic Kinetic Resolution
4.3 Racemization techniques
4.4 DKR of Chiral Alcohols
4.5 DKR of Chiral Amines
4.6 DKR of Other Compounds
5. Chemo-enzymatic Concurrent Deracemization
5.1 Deracemization of Amino acids and Amines
5.2 Deracemization of Hydroxy Acids and Alcohols
5.3 Deracemization of Chiral Sulfoxides
5.4 Summary and outlooks
6. One-pot Concurrent Chemo-Enzymatic Reactions
6.1 One-pot concurrent chemo-enzymatic cascades
6.1.1 Lipases
6.1.2 Carbonyl Reductases
6.1.3 Enoate Reductases
6.1.4 Transaminases
6.1.5 Monoamine Oxidases
6.1.6 Cytochrome P450s
6.1.7 Halohydrin Dehalogenases
6.1.8 Vanadium Haloperoxidases
6.1.9 Laccases
6.2 Integration of Chemical Reaction with Metabolism of Living Organisms
6.3 One-pot Concurrent Chemo-Enzymatic Cascades via Compartmentalization
6.4 Summary and outlooks
7. Photo-Catalytic and Biocatalytic Cascade Transformations
7.1 Photoenzymes
7.2 Light-Activation of Redox Enzymes without Co-factor Regeneration
7.3 Light-Activated Co-factor Regeneration for Redox Enzymes
7.4 Photo-Induced Catalytic Promiscuity of Redox Enzymes
7.5 Photocatalysis and Biocatalysis Cascades
7.5 Summary and outlooks
8. Perspectives
1.1 Advantages of Enzyme Catalysis
1.1.1 Chemo-selectivity
1.1.2 Regioselectivity
1.1.3 Stereoselectivity
1.1.4 Mild Reaction Conditions
1.2 Modes of Chemo-enzymatic transformations
1.2.1 "separate-pot-two-step" mode
1.2.2 "one-pot-two-step" mode
1.2.3 "one-pot-one-step" mode
1.3 Summary and outlooks
2 "Separate-Pot Two-Step" Chemo-Enzymatic Transformation
2.1 Lipases
2.2 Nitrilases
2.3 Carbonyl reductases
2.4 Ene reductases
2.5. Transaminases
2.6 Imine reductases
2.7 Cytochromes P450s
2.8 Baeyer-Villiger monooxygenases (BVMOs)
2.9 Aldolases
2.10 Epoxide hydrolases
2.11 Other Enzymes
2.12 Integration of Multi-Enzyme Cascade with Chemical Transformation
2.13 Summary and outlooks
3. One-Pot Sequential Chemoenzymatic Reactions
3.1 Lipases and Esterases
3.2 Carbonyl Reductases
3.3 Ene Reductases
3.4 Transaminases
3.5 Epoxide hydrolases (EHs)
3. 6 Other Enzymes
3.6.1 Aldolases
3.6.2 Halohydrin Dehalogenases
3.6.3 Phenylalanine Ammonia Lyases
3.6.4 D-amino Acid Dehydrogenases (DAADHs)
3.6.5 Halogenases
3.6.6 Imine Reductases
3.6.7 Decarboxylases
3.6.8 Cytochrome P450s
3.6.9 Hydroxynitrile Lyases
3.6.10 Nitrilases
3.6.11 Laccases
3.6.12 Transglutaminases
3.6.13 a-Ketoglutarate-Dependent (a-KG) non-Heme Iron Oxygenases
3.6.14 Galactose Oxidases
3.6.15 FAD-Dependent Monooxygenases
3.7 Summary and outlooks
4. Chemoenzymatic Dynamic Kinetic Resolution
4.1 Enzymatic Kinetic Resolution
4.2 Dynamic Kinetic Resolution
4.3 Racemization techniques
4.4 DKR of Chiral Alcohols
4.5 DKR of Chiral Amines
4.6 DKR of Other Compounds
5. Chemo-enzymatic Concurrent Deracemization
5.1 Deracemization of Amino acids and Amines
5.2 Deracemization of Hydroxy Acids and Alcohols
5.3 Deracemization of Chiral Sulfoxides
5.4 Summary and outlooks
6. One-pot Concurrent Chemo-Enzymatic Reactions
6.1 One-pot concurrent chemo-enzymatic cascades
6.1.1 Lipases
6.1.2 Carbonyl Reductases
6.1.3 Enoate Reductases
6.1.4 Transaminases
6.1.5 Monoamine Oxidases
6.1.6 Cytochrome P450s
6.1.7 Halohydrin Dehalogenases
6.1.8 Vanadium Haloperoxidases
6.1.9 Laccases
6.2 Integration of Chemical Reaction with Metabolism of Living Organisms
6.3 One-pot Concurrent Chemo-Enzymatic Cascades via Compartmentalization
6.4 Summary and outlooks
7. Photo-Catalytic and Biocatalytic Cascade Transformations
7.1 Photoenzymes
7.2 Light-Activation of Redox Enzymes without Co-factor Regeneration
7.3 Light-Activated Co-factor Regeneration for Redox Enzymes
7.4 Photo-Induced Catalytic Promiscuity of Redox Enzymes
7.5 Photocatalysis and Biocatalysis Cascades
7.5 Summary and outlooks
8. Perspectives
1 Introduction
1.1 Advantages of Enzyme Catalysis
1.1.1 Chemo-selectivity
1.1.2 Regioselectivity
1.1.3 Stereoselectivity
1.1.4 Mild Reaction Conditions
1.2 Modes of Chemo-enzymatic transformations
1.2.1 "separate-pot-two-step" mode
1.2.2 "one-pot-two-step" mode
1.2.3 "one-pot-one-step" mode
1.3 Summary and outlooks
2 "Separate-Pot Two-Step" Chemo-Enzymatic Transformation
2.1 Lipases
2.2 Nitrilases
2.3 Carbonyl reductases
2.4 Ene reductases
2.5. Transaminases
2.6 Imine reductases
2.7 Cytochromes P450s
2.8 Baeyer-Villiger monooxygenases (BVMOs)
2.9 Aldolases
2.10 Epoxide hydrolases
2.11 Other Enzymes
2.12 Integration of Multi-Enzyme Cascade with Chemical Transformation
2.13 Summary and outlooks
3. One-Pot Sequential Chemoenzymatic Reactions
3.1 Lipases and Esterases
3.2 Carbonyl Reductases
3.3 Ene Reductases
3.4 Transaminases
3.5 Epoxide hydrolases (EHs)
3. 6 Other Enzymes
3.6.1 Aldolases
3.6.2 Halohydrin Dehalogenases
3.6.3 Phenylalanine Ammonia Lyases
3.6.4 D-amino Acid Dehydrogenases (DAADHs)
3.6.5 Halogenases
3.6.6 Imine Reductases
3.6.7 Decarboxylases
3.6.8 Cytochrome P450s
3.6.9 Hydroxynitrile Lyases
3.6.10 Nitrilases
3.6.11 Laccases
3.6.12 Transglutaminases
3.6.13 a-Ketoglutarate-Dependent (a-KG) non-Heme Iron Oxygenases
3.6.14 Galactose Oxidases
3.6.15 FAD-Dependent Monooxygenases
3.7 Summary and outlooks
4. Chemoenzymatic Dynamic Kinetic Resolution
4.1 Enzymatic Kinetic Resolution
4.2 Dynamic Kinetic Resolution
4.3 Racemization techniques
4.4 DKR of Chiral Alcohols
4.5 DKR of Chiral Amines
4.6 DKR of Other Compounds
5. Chemo-enzymatic Concurrent Deracemization
5.1 Deracemization of Amino acids and Amines
5.2 Deracemization of Hydroxy Acids and Alcohols
5.3 Deracemization of Chiral Sulfoxides
5.4 Summary and outlooks
6. One-pot Concurrent Chemo-Enzymatic Reactions
6.1 One-pot concurrent chemo-enzymatic cascades
6.1.1 Lipases
6.1.2 Carbonyl Reductases
6.1.3 Enoate Reductases
6.1.4 Transaminases
6.1.5 Monoamine Oxidases
6.1.6 Cytochrome P450s
6.1.7 Halohydrin Dehalogenases
6.1.8 Vanadium Haloperoxidases
6.1.9 Laccases
6.2 Integration of Chemical Reaction with Metabolism of Living Organisms
6.3 One-pot Concurrent Chemo-Enzymatic Cascades via Compartmentalization
6.4 Summary and outlooks
7. Photo-Catalytic and Biocatalytic Cascade Transformations
7.1 Photoenzymes
7.2 Light-Activation of Redox Enzymes without Co-factor Regeneration
7.3 Light-Activated Co-factor Regeneration for Redox Enzymes
7.4 Photo-Induced Catalytic Promiscuity of Redox Enzymes
7.5 Photocatalysis and Biocatalysis Cascades
7.5 Summary and outlooks
8. Perspectives
1.1 Advantages of Enzyme Catalysis
1.1.1 Chemo-selectivity
1.1.2 Regioselectivity
1.1.3 Stereoselectivity
1.1.4 Mild Reaction Conditions
1.2 Modes of Chemo-enzymatic transformations
1.2.1 "separate-pot-two-step" mode
1.2.2 "one-pot-two-step" mode
1.2.3 "one-pot-one-step" mode
1.3 Summary and outlooks
2 "Separate-Pot Two-Step" Chemo-Enzymatic Transformation
2.1 Lipases
2.2 Nitrilases
2.3 Carbonyl reductases
2.4 Ene reductases
2.5. Transaminases
2.6 Imine reductases
2.7 Cytochromes P450s
2.8 Baeyer-Villiger monooxygenases (BVMOs)
2.9 Aldolases
2.10 Epoxide hydrolases
2.11 Other Enzymes
2.12 Integration of Multi-Enzyme Cascade with Chemical Transformation
2.13 Summary and outlooks
3. One-Pot Sequential Chemoenzymatic Reactions
3.1 Lipases and Esterases
3.2 Carbonyl Reductases
3.3 Ene Reductases
3.4 Transaminases
3.5 Epoxide hydrolases (EHs)
3. 6 Other Enzymes
3.6.1 Aldolases
3.6.2 Halohydrin Dehalogenases
3.6.3 Phenylalanine Ammonia Lyases
3.6.4 D-amino Acid Dehydrogenases (DAADHs)
3.6.5 Halogenases
3.6.6 Imine Reductases
3.6.7 Decarboxylases
3.6.8 Cytochrome P450s
3.6.9 Hydroxynitrile Lyases
3.6.10 Nitrilases
3.6.11 Laccases
3.6.12 Transglutaminases
3.6.13 a-Ketoglutarate-Dependent (a-KG) non-Heme Iron Oxygenases
3.6.14 Galactose Oxidases
3.6.15 FAD-Dependent Monooxygenases
3.7 Summary and outlooks
4. Chemoenzymatic Dynamic Kinetic Resolution
4.1 Enzymatic Kinetic Resolution
4.2 Dynamic Kinetic Resolution
4.3 Racemization techniques
4.4 DKR of Chiral Alcohols
4.5 DKR of Chiral Amines
4.6 DKR of Other Compounds
5. Chemo-enzymatic Concurrent Deracemization
5.1 Deracemization of Amino acids and Amines
5.2 Deracemization of Hydroxy Acids and Alcohols
5.3 Deracemization of Chiral Sulfoxides
5.4 Summary and outlooks
6. One-pot Concurrent Chemo-Enzymatic Reactions
6.1 One-pot concurrent chemo-enzymatic cascades
6.1.1 Lipases
6.1.2 Carbonyl Reductases
6.1.3 Enoate Reductases
6.1.4 Transaminases
6.1.5 Monoamine Oxidases
6.1.6 Cytochrome P450s
6.1.7 Halohydrin Dehalogenases
6.1.8 Vanadium Haloperoxidases
6.1.9 Laccases
6.2 Integration of Chemical Reaction with Metabolism of Living Organisms
6.3 One-pot Concurrent Chemo-Enzymatic Cascades via Compartmentalization
6.4 Summary and outlooks
7. Photo-Catalytic and Biocatalytic Cascade Transformations
7.1 Photoenzymes
7.2 Light-Activation of Redox Enzymes without Co-factor Regeneration
7.3 Light-Activated Co-factor Regeneration for Redox Enzymes
7.4 Photo-Induced Catalytic Promiscuity of Redox Enzymes
7.5 Photocatalysis and Biocatalysis Cascades
7.5 Summary and outlooks
8. Perspectives