Green Biocatalysis

Name: Green Biocatalysis
Brand: Wiley
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Ramesh N. Patel(Herausgeber*in)

Wiley (Verlag)

Erschienen am 9. Mai 2016

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Inhalt

Intro
Title Page
Copyright Page
Contents
Preface
About the Editor
Contributors
Chapter 1 Biocatalysis and Green Chemistry
1.1 INTRODUCTION TO SUSTAINABLE DEVELOPMENT AND GREEN CHEMISTRY
1.2 GREEN CHEMISTRY METRICS
1.3 ENVIRONMENTAL IMPACT AND SUSTAINABILITY METRICS
1.4 SOLVENTS
1.5 THE ROLE OF CATALYSIS
1.6 BIOCATALYSIS AND GREEN CHEMISTRY
1.7 EXAMPLES OF GREEN BIOCATALYTIC PROCESSES
1.7.1 A Chemoenzymatic Process for Pregabalin
1.7.2 A Three-Enzyme Process for Atorvastatin Intermediate
1.7.3 Enzymatic Synthesis of Sitagliptin
1.7.4 Biocatalytic Synthesis of the Fragrance Chemical (-) Ambrox (Ambrafuran)
1.8 CONCLUSIONS AND FUTURE PROSPECTS
REFERENCES
Chapter 2 Enzymatic Synthesis of Chiral Amines using ?-Transaminases, Amine Oxidases, and the Berberine Bridge Enzyme
2.1 INTRODUCTION
2.2 SYNTHESIS OF CHIRAL AMINES USING ?-TRANSAMINASES
2.2.1 ?-Transaminases: Definition and General Facts
2.2.2 Stereoselective Transformations Involving ?-TAs
2.2.3 Asymmetric Amination of Ketones
2.2.4 Asymmetric Amination of Linear Ketones
2.2.5 Asymmetric Amination of Cyclic Ketones
2.2.6 Application in the Synthesis of Pharmaceutically Active Ingredients
2.2.7 Amination of Ketones in Organic Solvents
2.2.8 Asymmetric Amination of Keto Acids: Synthesis of Nonnatural Amino Acids
2.2.9 Amination of Aldehydes
2.2.10 Cascade Reactions Involving ?-TAs
2.2.11 Cascades Initiated by ?-TAs: Synthesis of Chiral Heterocycles
2.2.12 Multienzyme Cascades Involving ?-TA-Catalyzed Amination of Ketones
2.2.13 Deracemization of Primary Amines
2.2.14 Perspective
2.3 AMINE OXIDASES
2.3.1 Amino Acid Oxidases
2.3.2 Cascade Reactions Involving AAOs
2.3.3 Monoamine Oxidases
2.3.4 Cascade Reactions Involving Monoamine Oxidases
2.3.5 Perspective
2.4 BERBERINE BRIDGE ENZYMES
2.5 CONCLUSIONS
REFERENCES
Chapter 3 Decarboxylation and Racemization of Unnatural Compounds using Artificial Enzymes Derived from Arylmalonate Decarboxylase
3.1 INTRODUCTION
3.2 DISCOVERY OF A BACTERIAL a-ARYL-a-METHYLMALONATE DECARBOXYLASE
3.3 PURIFICATION AND CHARACTERIZATION OF THE DECARBOXYLASE (AMDase)
3.4 CLONING OF THE AMDase GENE
3.5 STEREOCHEMICAL COURSE OF AMDase-CATALYZED DECARBOXYLATION
3.6 DIRECTED EVOLUTION OF AMDase TO AN ARTIFICIAL PROFEN RACEMASE
3.7 INVERSION OF ENANTIOSELECTIVITY DRAMATICALLY IMPROVES CATALYTIC ACTIVITY
3.8 FUTURE PROSPECTS
REFERENCES
Chapter 4 Green Processes for the Synthesis of Chiral Intermediates for the Development of Drugs
4.1 INTRODUCTION
4.2 SAXAGLIPTIN: ENZYMATIC SYNTHESIS OF (S)-N-BOC-3-HYDROXYADAMANTYLGLYCINE
4.3 SITAGLIPTIN: ENZYMATIC SYNTHESIS OF CHIRAL AMINE
4.4 VANLEV: ENZYMATIC SYNTHESIS OF (S)-6-HYDROXYNORLEUCINE
4.5 VANLEV: ENZYMATIC SYNTHESIS OF ALLYSINE ETHYLENE ACETAL
4.6 VANLEV: ENZYMATIC SYNTHESIS OF THIAZEPINE
4.7 TIGEMONAM: ENZYMATIC SYNTHESIS OF (S)-ß-HYDROXYVALINE
4.8 AUTOIMMUNE DISEASES: ENZYMATIC SYNTHESIS OF (S)-NEOPENTYLGLYCINE
4.9 ATAZANAVIR: ENZYMATIC SYNTHESIS OF (S)-TERTIARY LEUCINE
4.10 THROMBIN INHIBITOR (INOGATRAN): SYNTHESIS OF (R)-CYCLOHEXYLALANINE
4.11 GAMMA SECRETASE INHIBITOR: ENZYMATIC SYNTHESIS OF (R)-5,5,5-TRIFLUORONORVALINE
4.12 NK1/NK2 DUAL ANTAGONISTS: ENZYMATIC DESYMMETRIZATION OF DIETHYL 3-[3',4'-DICHLOROPHENYL] GLUTARATE
4.13 PREGABALIN: ENZYMATIC SYNTHESIS OF ETHYL (S)-3-CYANO-5-METHYLHEXANOATE
4.14 CHEMOKINE RECEPTOR MODULATOR: ENZYMATIC SYNTHESIS OF (1S,2R)-2-(METHOXYCARBONYL)CYCLOHEX- 4-ENE-1-CARBOXYLIC ACID
4.15 ENZYMATIC SYNTHESIS OF (3S,5R)-3-(AMINOMETHYL)- 5-METHYLOCTANOIC ACID
4.16 ATORVASTATIN (LIPITOR): ENZYMATIC DESYMMETRIZATION OF 3-HYDROXYGLUTARONITRILE
4.17 ANTICANCER DRUGS: ENZYMATIC SYNTHESIS OF TAXANE SIDE CHAIN
4.18 ANTIDIABETIC AND CNS DRUGS: ENZYMATIC HYDROLYSIS OF DIMETHYL BICYCLO[2.2.1]HEPTANE-1,4-DICARBOXYLATE
4.19 CLOPIDOGREL (PLAVIX): ENZYMATIC PREPARATION OF 2-CHLOROMANDELIC ACID ESTERS
4.20 aNTIVIRAL DRUG: REGIOSELECTIVE ENZYMATIC ACYLATION OF RIBAVIRIN
4.21 ANTICHOLESTEROL DRUG: ENZYMATIC ACYLATION OF ALCOHOL
4.22 SAXAGLIPTIN: ENZYMATIC SYNTHESIS OF (5S)-4,5-DIHYDRO-1H-PYRROLE-1,5 DICARBOXYLIC ACID, 1-(1,1-DIMETHYLETHYL)-5-ETHYL ESTER
4.23 MONTELUKAST: SYNTHESIS OF INTERMEDIATE FOR LTD4 ANTAGONISTS
4.24 ATAZANAVIR: ENZYMATIC SYNTHESIS OF (1S,2R)- [3-CHLORO-2-HYDROXY-1 (PHENYLMETHYL) PROPYL]-CARBAMIC ACID,1,1-DIMETHYL-ETHYL ESTER
4.25 ATORVASTATIN: ENZYMATIC SYNTHESIS OF (R)-4-CYANO-3-HYDROXYBUTYRATE
4.26 ANTIANXIETY DRUG: ENZYMATIC SYNTHESIS OF 6-HYDROXYBUSPIRONE
4.27 PROTEASE INHIBITOR: ENZYMATIC SYNTHESIS OF (R)-3-(4-FLUOROPHENYL)-2-HYDROXY PROPIONIC ACID
4.28 DERMATOLOGICAL AND ANTICANCER DRUGS: ENZYMATIC SYNTHESIS OF 2-(R)-HYDROXY-2-(1',2',3',4'-TETRAHYDRO-1',1',4',4'-TETRAMETHYL-6'-NAPHTHALENYL)ACETATE
4.29 ANTIPSYCHOTIC DRUG: ENZYMATIC REDUCTION OF 1-(4-FLUOROPHENYL)4-[4-(5-FLUORO-2-PYRIMIDINYL) 1-PIPERAZINYL]-1-BUTANONE
4.30 CHOLESTEROL-LOWERING AGENTS: ENZYMATIC SYNTHESIS OF (3S,5R)-DIHYDROXY-6-(BENZYLOXY) HEXANOIC ACID, ETHYL ESTER
4.31 ANTIMIGRAINE DRUGS: ENZYMATIC SYNTHESIS OF (R)-2-AMINO-3-(7-METHYL-1H-INDAZOL-5-YL) PROPANOIC ACID
4.32 ANTIDIABETIC DRUG (GLP-1 MIMICS): ENZYMATIC SYNTHESIS OF (S)-AMINO-3-[3-{6-(2-METHYLPHENYL)} PYRIDYL]-PROPIONIC ACID
4.33 EPHEDRINE: SYNTHESIS OF (R)-PHENYLACETYLCARBINOL
4.34 ZANAMIVIR: ENZYMATIC SYNTHESIS OF N-ACETYLNEURAMINIC ACID
4.35 EPIVIR: ENZYMATIC DEAMINATION PROCESS FOR THE SYNTHESIS OF (2´R-CIS)-2´-DEOXY-3-THIACYTIDINE
4.36 HMG-CoA REDUCTASE INHIBITORS: ALDOLASE-CATALYZED SYNTHESIS OF CHIRAL LACTOL
4.37 BOCEPREVIR: OXIDATION OF 6,6-DIMETHYL-3-AZABICYCLO[3.1.0]HEXANE BY MONOAMINE OXIDASE
4.38 CRIXIVAN: ENZYMATIC SYNTHESIS OF INDANDIOLS
4.39 POTASSIUM CHANNEL OPENER: PREPARATION OF CHIRAL EPOXIDE AND TRANS-DIOL
4.40 EPOTHILONES (ANTICANCER DRUGS): EPOTHILONE B AND EPOTHILONE F
4.41 ß-ADRENERGIC BLOCKING AGENTS: SYNTHESIS OF INTERMEDIATES FOR PROPRANOLOL AND DENOPAMINE
4.42 CONCLUSION
REFERENCES
Chapter 5 Dynamic Kinetic Resolution of Alcohols, Amines, and Amino Acids
5.1 INTRODUCTION
5.1.1 Kinetic and Dynamic Kinetic Resolution
5.1.2 Enzymes as the Resolution Catalysts for DKR
5.1.3 The Enantioselectivity of Enzymes in DKR
5.1.4 Metal (Complexes) as the Racemization Catalysts for DKR
5.2 DYNAMIC KINETIC RESOLUTION OF SECONDARY ALCOHOLS
5.3 DYNAMIC KINETIC RESOLUTION OF AMINES AND AMINO ACIDS
5.4 APPLICATIONS OF DYNAMIC KINETIC RESOLUTION
5.5 SUMMARY
APPENDIX: LIST OF ABBREVIATIONS
REFERENCES
Chapter 6 Recent Developments in Flavin-Based Catalysis: Enzymatic Sulfoxidation
6.1 INTRODUCTION
6.2 ENZYMATIC SULFOXIDATION CATALYZED BY FLAVOPROTEIN OXIDASES
6.3 USE OF FLAVOPROTEIN MONOOXYGENASES FOR THE SYNTHESIS OF CHIRAL SULFOXIDES
6.3.1 Sulfoxidations Catalyzed by Baeyer-Villiger Monooxygenases
6.3.2 Oxidative Processes Employing Styrene Monooxygenases
6.3.3 Enzymatic Sulfoxidations Catalyzed by Flavin-Containing Monooxygenases
6.4 ASYMMETRIC SULFOXIDATION USING FLAVINS AS CATALYSTS
6.5 SUMMARY AND OUTLOOK
REFERENCES
Chapter 7 Development of Chemoenzymatic Processes: An Industrial Perspective
7.1 INTRODUCTION
7.2 SYNTHETIC ROUTE DESIGN AND INTEGRATION OF BIOCATALYSIS
7.3 SCREENING AND BIOCATALYST SELECTION
7.4 CHEMOENZYMATIC PROCESS DEVELOPMENT
7.4.1 Reaction Engineering versus Enzyme Engineering
7.4.2 Product Isolation
7.4.3 Scale-Up of Enzymatic Processes
7.4.4 Enzyme Supply Scenarios
7.4.5 Manufacture of APIs using Enzymes: Quality and Safety Aspects
7.5 CONCLUSIONS
REFERENCES
Chapter 8 Epoxide Hydrolases and their Application in Organic Synthesis
8.1 INTRODUCTION
8.2 SOURCES AND REACTION MECHANISM OF EHs
8.2.1 Sources of EHs
8.2.2 Heterologous Expression of EHs
8.2.3 Reaction Mechanisms of EHs
8.3 DIRECTED EVOLUTION AND GENETIC ENGINEERING OF EHs
8.4 IMMOBILIZED EHs AND REACTIONS IN NONAQUEOUS MEDIA
8.4.1 Immobilization of EHs
8.4.2 EH-Catalyzed Reactions in Organic Solvent- or Ionic Liquid-Containing Media
8.5 MONOFUNCTIONAL EPOXIDES AS CHIRAL BUILDING BLOCKS FOR THE SYNTHESIS OF BIOLOGICALLY ACTIVE COMPOUNDS
8.5.1 Monosubstituted Aromatic Epoxides
8.5.2 Disubstituted Aromatic Epoxides
8.5.3 Nonaromatic Epoxides
8.5.4 meso-Epoxides
8.6 PREPARATION OF VALUABLE CHIRAL BUILDING BLOCKS FOR THE SYNTHESIS OF BIOLOGICALLY ACTIVE COMPOUNDS STARTING FROM BIFUNCTIONAL EPOXIDES
8.6.1 Halogenated Epoxides
8.6.2 Epoxyamide
8.6.3 Protected Epoxy Alcohols
8.6.4 Epoxy Ester
8.6.5 Epoxy Aldehyde
8.7 APPLICATION TO NATURAL PRODUCT SYNTHESIS
8.7.1 Disparlure
8.7.2 Linalool
8.7.3 Bisabolol
8.7.4 Frontalin
8.7.5 Mevalonolactone
8.7.6 Myrcenediol and Beer Aroma
8.7.7 Pityol
8.7.8 Pestalotin: Jamaican Rum Constituent
8.7.9 Panaxytriol
8.7.10 Fridamycin E
8.8 BIENZYMATIC PROCESS IMPLYING ONE EPOXIDE HYDROLASE
8.9 CONCLUSIONS
REFERENCES
Chapter 9 Enantioselective Acylation of Alcohol and Amine Reactions in Organic Synthesis
9.1 INTRODUCTION
9.1.1 General Considerations for Hydrolase-Catalyzed Reactions
9.1.2 Serine Hydrolase Mechanism for the Acylation of Alcohols and Amines
9.1.3 Use of Organic Solvents for Hydrolase-Catalyzed Acylation Reactions
9.2 ENANTIOSELECTIVE ACYLATION OF ALCOHOLS
9.2.1 Classical Kinetic Resolution of Racemic Alcohols
9.2.2 Dynamic Kinetic Resolution of Racemic Alcohols
9.2.3 Desymmetrization of Diols
9.2.4 Selected Examples of Acylation Reaction with Interest for the Pharmaceutical Industry
9.3 ACYLATION OF AMINES
9.3.1 Kinetic Resolution of Racemic Amines
9.3.2 Dynamic Kinetic Resolution of Racemic Amines
9.3.3 Selected Examples of Acylation Reactions with Interest for the Pharmaceutical Industry
9.4 CONCLUSIONS
REFERENCES
Chapter 10 Recent Advances in Enzyme-Catalyzed Aldol Addition Reactions
10.1 INTRODUCTION
10.2 PYRUVATE-DEPENDENT ALDOLASES
10.2.1 N-Acetylneuraminic Acid Aldolase
10.2.2 Other Pyruvate-Dependent Aldolases
10.2.3 Structure-Guided Pyruvate Aldolase Modification
10.3 DIHYDROXYACETONE PHOSPHATE (DHAP)-DEPENDENT ALDOLASES, d-FRUCTOSE-6-PHOSPHATE ALDOLASE (FSA) AND TRANSALDOLASES
10.3.1 DHAP-Dependent Aldolases
10.3.2 Iminocyclitol, Pipecolic Acids, Homoiminocyclitols, and Aminocyclitol Synthesis
10.3.3 Synthesis of Polyhydroxylated Pipecolic Acids and Homoiminocyclitols
10.3.4 Aminocyclitol Synthesis
10.3.5 DHA-Utilizing Enzymes
10.3.6 Iminocyclitol, Pipecolic Acid, Homoiminocyclitols, and Aminocyclitol Synthesis
10.3.7 Carbohydrates, Deoxysugars, and Sugar Phosphate Synthesis
10.4 THREONINE ALDOLASES
10.4.1 2-Deoxy-d-Ribose 5-Phosphate Aldolase
10.5 ALDOL TYPE REACTIONS CATALYZED BY NON-ALDOLASES
10.6 COMPUTATIONAL DE NOVO ENZYME DESIGN
10.7 CONCLUSIONS AND PERSPECTIVES
REFERENCES
Chapter 11 Enzymatic Asymmetric Reduction of Carbonyl Compounds
11.1 INTRODUCTION
11.2 MECHANISMS
11.3 PREPARATION OF BIOCATALYSTS
11.3.1 Screening of Enzymes from Culturable Microorganisms
11.3.2 Screening of Enzymes using Metagenomes
11.3.3 Screening of Enzymes of Microorganisms of Known Genome Data
11.3.4 Mutation of Enzymes
11.3.5 Hyperthermophilic Enzyme as a Biocatalyst
11.3.6 Photosynthetic Organism as a Biocatalyst "Photobiocatalyst"
11.4 SOLVENT ENGINEERING
11.4.1 Organic Solvent
11.4.2 CO2
11.4.3 Ionic Liquid
11.5 EXAMPLES FOR BIOCATALYTIC ASYMMETRIC REDUCTIONS
11.5.1 Reduction of Ketones
11.5.2 Reduction of Diketones
11.5.3 Dynamic Kinetic Resolution Through Reduction
11.6 CONCLUSIONS
REFERENCES
Chapter 12 Nitrile-Converting Enzymes and their Synthetic Applications
12.1 INTRODUCTION
12.2 SCREENING METHODOLOGY
12.2.1 Screening Metagenomic Libraries
12.2.2 Database Mining
12.2.3 Construction of Enzyme Variants
12.3 NITRILASES
12.3.1 Arylacetonitrilases
12.3.2 Aromatic Nitrilases
12.3.3 Aliphatic Nitrilases
12.3.4 Plant Nitrilases and their Bacterial Homologues
12.4 NITRILE HYDRATASES
12.4.1 Fe-type Nitrile Hydratase
12.4.2 Co-type Nitrile Hydratase
12.5 CONCLUSIONS
ACKNOWLEDGEMENTS
REFERENCES
Chapter 13 Biocatalytic Epoxidation for Green Synthesis
13.1 INTRODUCTION
13.2 ENZYMES FOR ASYMMETRIC EPOXIDATION
13.2.1 Monooxygenases
13.2.2 Chloroperoxidases
13.3 APPLICATION OF BIOEPOXIDATION IN ORGANIC SYNTHESIS
13.3.1 Asymmetric Epoxidation of Aliphatic Alkenes
13.3.2 Asymmetric Epoxidation of Aromatic Alkenes
13.4 PROTEIN ENGINEERING FOR BIOCATALYTIC EPOXIDATION REACTION
13.4.1 Screening Methods
13.4.2 Examples of Engineered Enzymes for Biocatalytic Epoxidation Reactions
13.5 CONCLUSIONS AND OUTLOOK
ACKNOWLEDGMENTS
REFERENCES
Chapter 14 Dynamic Kinetic Resolution via Hydrolase-Metal Combo Catalysis
14.1 INTRODUCTION
14.2 DKR OF SECONDARY ALCOHOLS
14.2.1 Racemization Catalysts for DKR of sec-Alcohols
14.2.2 Synthetic Applications of the DKR of sec-Alcohols
14.3 DKR OF AMINES
14.3.1 Racemization Catalyst for the DKR of Amines
14.3.2 Synthetic Applications of the DKR of Amines
14.4 CONCLUSION
REFERENCES
Chapter 15 Discovery and Engineering of Enzymes for Peptide Synthesis and Activation
15.1 INTRODUCTION
15.2 CLASSIFICATION OF ENZYMES FOR PEPTIDE COUPLING
15.3 SERINE AND CYSTEINE PROTEASES FOR PEPTIDE SYNTHESIS
15.3.1 Chymotrypsin, Trypsin, and Related Enzymes
15.3.2 Subtilisin-Like Enzymes
15.3.3 Other Serine Hydrolases
15.3.4 Aminopeptidases
15.3.5 Peptidases Accepting ß-Amino Acids
15.3.6 d-Amino Acid-Specific Peptidases
15.3.7 Sulfhydryl Peptidases
15.3.8 Sortase
15.3.9 Metalloproteases in Peptide Synthesis
15.3.10 Aspartic Proteases in Peptide Synthesis
15.4 PROTEASE DISCOVERY
15.4.1 Metagenomics
15.4.2 Proteases from Thermophiles
15.4.3 Solvent-Tolerant Proteases
15.4.4 Proteases from Salt-Resistant Organisms
15.5 PROTEASES ENGINEERED FOR IMPROVED SYNTHESIS
15.5.1 Solvent-Resistant and Thermostable Subtilase Mutants
15.5.2 Thermostable Thermolysin Variants
15.5.3 Increasing Aminolysis to Hydrolysis Ratio by Protein Engineering
15.5.4 Protein Engineering of Trypsin-Like Proteases
15.5.5 Computational Design
15.6 ENZYMES FOR PEPTIDE TERMINAL MODIFICATION
15.6.1 Subtilisins for C-Terminal Peptide Modification
15.6.2 C-Terminal Activation by Lipase
15.6.3 Peptide Deformylase
15.6.4 Peptide Amidases for C-Terminal Modification
15.6.5 Enzymes for N-Terminal Modification
15.6.6 Enzymes for Peptide Cyclization
15.7 CONCLUSIONS
REFERENCES
Chapter 16 Biocatalysis for Drug Discovery and Development
16.1 INTRODUCTION
16.2 SINGLE ENZYMATIC REACTIONS
16.2.1 Hydrolytic Reaction
16.2.2 Reduction
16.2.3 Oxidation
16.2.4 C-C Bond-Forming Reaction
16.2.5 Michael-Type Reaction
16.2.6 Diels-Alder Reaction
16.2.7 Pictet-Spengler Reaction
16.2.8 Terpene Cyclization
16.2.9 Transfer Reaction
16.2.10 Fluorination
16.2.11 Other Reactions
16.2.12 Bifunctional Enzymes
16.3 MULTIENZYME BIOCATALYTIC REACTIONS
16.3.1 One-Pot Cascade Reactions
16.3.2 Whole-Cell Biocatalysts
16.3.3 Multistep Biocatalytic Conversions
16.4 FUTURE PERSPECTIVE: BIOCATALYSTS FOR THE PHARMACEUTICAL INDUSTRY
16.4.1 Biocatalyst Discovery: New Enzymes, New Chemistries
16.4.2 Biocatalyst Development: Improvement of Desired Properties
16.4.3 Integration of Biocatalytic Processes
16.5 CONCLUSION
REFERENCES
Chapter 17 Application of Aromatic Hydrocarbon Dioxygenases
17.1 INTRODUCTION
17.2 CHALLENGES IN AROMATIC HYDROCARBON DIOXYGENASE APPLICATIONS
17.3 PROTEIN ENGINEERING TO IMPROVE ENZYMATIC ACTIVITY AND ALTER SUBSTRATE SPECIFICITY
17.4 PROTEIN ENGINEERING FOR THE PRODUCTION OF SPECIFIC CHEMICALS
17.5 STRAIN MODIFICATION FOR THE DEVELOPMENT OF NEW BIODEGRADATION PATHWAYS
17.6 PHYTOREMEDIATION: THE EXPRESSION OF BACTERIAL DIOXYGENASES IN PLANT SYSTEMS FOR BIOREMEDIATION PURPOSES
17.7 CONCLUDING REMARKS
ACKNOWLEDGMENTS
REFERENCES
Chapter 18 Ene-reductases and their Applications
18.1 INTRODUCTION
18.2 SUBSTRATE CLASSES AND INDUSTRIAL APPLICATIONS
18.3 MULTIENZYME REACTIONS
18.4 ALTERNATIVE HYDRIDE SOURCES
18.5 IMPROVEMENTS OF PRODUCTIVITY, STEREOSELECTIVITY, AND/OR CONVERSION
REFERENCES
Chapter 19 Recent Developments in Aminopeptidases, Racemases, and Oxidases
19.1 AMINOPEPTIDASE
19.1.1 Discovery of d-Stereospecific Aminopeptidase and its Utilization for Dynamic Kinetic Resolution
19.1.2 Discovery of d-Aminopeptidase, d-Amino Acid Amidase, and Alkaline d-Peptidase
19.1.3 Structure of d-Aminopeptidase (DAP)
19.1.4 Structure of d-Amino Acid Amidase (DaaA)
19.2 RACEMASE
19.2.1 Synthesis of d-Amino Acids by Optical Resolution and Dynamic Kinetic Resolution
19.2.2 Structure of ACL Racemase
19.2.3 In Silico Identification of ACL Racemases
19.3 AMINO ACID OXIDASE
19.3.1 Development of Novel R-Stereoselective Amine Oxidase
19.3.2 Design of R-Stereoselective Amine Oxidase
19.3.3 Deracemization Reaction with R-Stereoselective AOx
19.3.4 Structure of the Mutant Porcine Kidney d-Amino Acid Oxidase (Y228L, R283G)
REFERENCES
Chapter 20 Biocatalytic Cascades for API Synthesis
20.1 INTRODUCTION
20.2 MULTIENZYMATIC BIOCATALYSIS
20.2.1 Rationale
20.2.2 Biocatalytic Cascade Concepts
20.3 PROCESS ASPECTS FOR MULTISTEP BIOCATALYSIS
20.3.1 Balancing Reaction Schemes
20.3.2 Biocatalytic Reactor Options
20.3.3 Process Intensification
20.3.4 Continuous Processes
20.3.5 Process Integration
20.4 PROCESS DEVELOPMENT
20.5 BIOCATALYTIC CASCADE EXAMPLES
20.5.1 Linear Cascades
20.5.2 Parallel Cascades
20.5.3 Cyclic Cascades
20.5.4 Orthogonal Cascades
20.5.5 Linear-Parallel
20.5.6 Linear-Cyclic
20.5.7 Complex Cascades
20.5.8 Convergent Parallel Cascade
20.6 FUTURE OUTLOOK
20.6.1 Protein Engineering
20.6.2 Flow Chemistry and Process Intensification
REFERENCES
Chapter 21 Yeast-Mediated Stereoselective Synthesis
21.1 INTRODUCTION
21.2 REDUCTIONS OF ALDEHYDES AND KETONES
21.3 REDUCTION OF THIOCARBONYLS OR SULFUR-CONTAINING COMPOUNDS
21.4 REDUCTION OF FUNCTIONALIZED CARBONYL AND DICARBONYL COMPOUNDS
21.5 REDUCTION OF KETO ESTERS
21.6 HYDROLYSIS OF ESTERS
21.7 IMMOBILIZED BAKER'S YEAST
21.8 WHOLE-CELL BIOCATALYSIS IN IONIC LIQUIDS AND DEEP EUTECTIC SOLVENTS
21.9 C-C BOND-FORMING AND BREAKING REACTIONS
21.10 MISCELLANEOUS REACTIONS
21.11 CONCLUSIONS
REFERENCES
Chapter 22 Biocatalytic Introduction of Chiral Hydroxy Groups using Oxygenases and Hydratases
22.1 INTRODUCTION
22.2 REGIO- AND STEREOSELECTIVE HYDROXYLATION OF PROPYLBENZENE AND 3-CHLOROSTYRENE BY CYTOCHROME P450 BM-3 AND ITS MUTANT
22.3 REGIO- AND STEREOSELECTIVE HYDROXYLATION OF ALIPHATIC AMINO ACIDS BY FE(II)/a-KETOGLUTARATE-DEPENDENT DIOXYGENASES
22.3.1 l-Isoleucine 4-Hydroxylase
22.3.2 Fe/aKG-DOs Closely Homologous with l-Isoleucine 4-Hydroxylase
22.3.3 l-Leucine 5-Hydroxylase
22.3.4 N-Succinyl l-Leucine 3-Hydroxylase
22.3.5 Catalytic Properties of the Aliphatic Amino Acid Hydroxylases
22.3.6 Practical Use of Fe(II)/a-Ketoglutarate-Dependent Dioxygenases Coupled with Cosubstrate Generation System
22.4 REGIO- AND STEREOSELECTIVE HYDRATION OF UNSATURATED FATTY ACIDS BY A NOVEL FATTY ACID HYDRATASE
22.4.1 Linoleic Acid ?9 Hydratase
22.4.2 Efficient Enzymatic Production of Hydroxy Fatty Acids by Linoleic Acid ?9 Hydratase
22.5 CONCLUSION
ACKNOWLEDGMENT
REFERENCES
Chapter 23 Asymmetric Synthesis with Recombinant Whole-Cell Catalysts
23.1 INTRODUCTION
23.2 THE DESIGN/CONSTRUCTION OF WHOLE-CELL CATALYSTS
23.3 BIOTRANSFORMATIONS WITH WHOLE-CELL CATALYSTS
23.3.1 Hydrolysis Reactions
23.3.2 Hydration and Dehydration Reactions
23.3.3 C-C Bond-Forming Reactions
23.3.4 Reduction Reactions
23.3.5 Oxidation Reactions
23.4 CONCLUSION
REFERENCES
Chapter 24 Lipases and Esterases as User-Friendly Biocatalysts in Natural Product Synthesis
24.1 INTRODUCTION
24.2 DESYMMETRIZATION OF PROCHIRAL OR meso-DIOLS AND DIACETATES
24.2.1 Desymmetrization of meso-Compounds with 1,2-Stereogenic Centers
24.2.2 Desymmetrization of meso-Compounds with 1,3- and 1,5-Stereogenic Centers
24.2.3 Desymmetrization of Prochiral Compounds with a Single Stereogenic Center
24.3 KINETIC RESOLUTION OF RACEMIC ALCOHOLS
24.3.1 Kinetic Resolution of (±)-Primary Alcohols
24.3.2 Kinetic Resolution of Acyclic (±)-Secondary Alcohols
24.3.3 Kinetic Resolution of Cyclic (±)-Secondary Alcohols
24.4 PREPARATION OF ENANTIOPURE INTERMEDIATE(S) FROM A MIXTURE OF STEREOISOMERS
24.4.1 (1S,4R)-4-t-Butyldimethylsilyloxy-3-Chloro-2-Cyclopenten-1-ol (54)
24.4.2 (4R,5S)-5-Hydroxy-4-Methyl-3-Hexanone (55)
24.4.3 (3R,14R,26R)-3,26-Diacetoxy-14-Methyl-1,2-bis(trimethylsilyl)octacosa-4,24-Diene-1,27-Diyne (60)
24.5 CONCLUSION
ACKNOWLEDGMENTS
REFERENCES
Chapter 25 Hydroxynitrile Lyases for Biocatalytic Synthesis of Chiral Cyanohydrins
25.1 INTRODUCTION
25.2 DISCOVERY OF HYDROXYNITRILE LYASES: BIOPROSPECTING
25.2.1 Screening Plants Based on Detection of Activity
25.2.2 Isolation of HNL Proteins and Identification of the Encoding Genes
25.2.3 Database Mining
25.2.4 Heterologous Expression
25.3 APPLICATIONS OF HYDROXYNITRILE LYASES
25.3.1 Cyanohydrins
25.3.2 ß-Nitro Alcohols
25.4 STRUCTURAL AND MECHANISTIC ASPECTS
25.5 ENGINEERING OF HYDROXYNITRILE LYASES
25.5.1 Substrate Scope, Activity, and Enantioselectivity
25.5.2 Stability
25.5.3 Expression
25.5.4 New Catalytic Activities
25.6 REACTION ENGINEERING AND REACTION SYSTEMS
25.6.1 Reaction Systems
25.6.2 Immobilization of HNLs
25.7 CONCLUSION
ACKNOWLEDGMENT
REFERENCES
Chapter 26 Biocatalysis: Nitrilases in Organic Synthesis
26.1 INTRODUCTION
26.2 NITRILASE DISCOVERY
26.2.1 Conventional Screening
26.2.2 Metagenomic Mining
26.2.3 Genome Mining
26.3 NITRILASE IMPROVEMENT
26.3.1 Culture Optimization
26.3.2 Nitrilase Reengineering
26.4 APPLICATIONS IN ORGANIC SYNTHESIS
26.4.1 Production of Glycolic Acid
26.4.2 Production of Iminodiacetic Acid
26.4.3 Production of Indole-3-Acetic Acid
26.4.4 Conversion of Phenylacetonitrile and its Derivates
26.4.5 Regioselective Hydrolysis of Dinitriles
26.4.6 Degradation of Benzonitrile Herbicides
26.5 CONCLUSIONS AND FUTURE PROSPECTS
ACKNOWLEDGMENTS
REFERENCES
Chapter 27 Biotechnology for the Production of Chemicals, Intermediates, and Pharmaceutical Ingredients
27.1 INTRODUCTION
27.2 VALUE CHAINS AND MARKETS
27.2.1 Pharmaceuticals
27.2.2 Medical Technology (MedTech)
27.2.3 Food and Feed
27.2.4 Flavor and Fragrance
27.2.5 Cosmetics and Personal Care
27.2.6 Polymers
27.2.7 Surfactants and Lubricants
27.2.8 Commodity Chemicals
27.2.9 Energy
27.2.10 Other Markets and Products
27.3 THE TOOLBOX
27.3.1 The Current Toolbox
27.3.2 The Future Toolbox
27.4 SUSTAINABILITY, GREEN PREMIUM PRICING, AND SUBSIDIES
27.5 REGULATORY ASPECTS AND PUBLIC PERCEPTION
27.6 INNOVATION (NOT ONLY IN THE LABORATORY!)
27.7 CONCLUSIONS
ACKNOWLEDGMENTS
REFERENCES
Chapter 28 Microbial Transformations of Pentacyclic Triterpenes
28.1 INTRODUCTION
28.2 TYPICAL BIOTRANSFORMATIONS IN THE LUPANE FAMILY
28.3 TYPICAL BIOTRANSFORMATIONS IN THE OLEANE FAMILY
28.4 TYPICAL BIOTRANSFORMATIONS IN THE URSANE FAMILY
28.5 MICROBIAL TRANSFORMATIONS OF OTHER PTs
28.6 GLYCOSYLATIONS AND DEGLYCOSYLATIONs
28.7 CONCLUSION AND PERSPECTIVES
REFERENCES
Chapter 29 Transaminases and their Applications
29.1 INTRODUCTION
29.2 GENERAL PROPERTIES OF TRANSAMINASES
29.2.1 Classification as Pyridoxal-5'-Phosphate-Dependent Enzymes
29.2.2 Classification Based on Substrate Scope
29.2.3 Reaction Mechanism
29.2.4 Enantioselectivity of Transaminases
29.3 SYNTHESIS STRATEGIES WITH TRANSAMINASES
29.3.1 Synthesis of Chiral Amines
29.3.2 Synthesis of Canonical and Noncanonical Amino Acids
29.3.3 Synthesis of ß-Amino Acids
29.3.4 Synthesis of Amino Alcohols
29.3.5 Transaminase-Catalyzed Reactions with Whole Cells
29.4 APPROACHES TO OPTIMIZE THE TRANSAMINASE-CATALYZED REACTIONS
29.4.1 Protein Engineering by Rational Enzyme Design
29.4.2 Protein Engineering by Directed Evolution
29.4.3 Immobilization of Transaminases
29.4.4 Process Development: A Fast Way to Identify Appropriate Transaminases
29.4.5 ?-Transaminases in Organic Solvents
29.5 CONCLUSION
REFERENCES
Index
EULA

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