http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
This book explores the field of biocatalysis and its application in asymmetric synthesis, providing a comprehensive overview of enzymatic processes used to generate chirality in chemical compounds. Edited by Gonzalo de Gonzalo and Andrés R. Alcántara, it delves into various enzymatic methods such as hydrolases, reductases, and oxidases, focusing on their role in green chemistry and sustainable practices. The work discusses the latest advancements in protein and medium engineering, computational methods for stereocontrol, and industrial applications of biocatalysis in the manufacture of chiral compounds. It is intended for researchers, practitioners, and students in organic chemistry and biocatalysis, aiming to enhance their understanding of cutting-edge biocatalytic techniques and their industrial relevance.
Front Cover -- Biocatalysis in Asymmetric Synthesis -- Copyright Page -- Contents -- List of contributors -- About the editors -- Preface -- 1 Introduction to asymmetric synthesis employing biocatalysts -- 1.1 Introduction -- 1.2 Type of enzymatic processes for generating asymmetry -- 1.2.1 Chirality associated to sp3 carbon atoms -- 1.2.1.1 Kinetic resolutions (KRs) -- 1.2.1.2 Parallel kinetic resolutions -- 1.2.1.3 Deracemizations -- 1.2.1.4 Enantioconvergent processes -- 1.2.1.5 Dynamic kinetic resolutions -- 1.2.2 Pro-chirality associated to sp2 carbon atoms -- 1.3 Biocatalysts preparations -- 1.4 Novel-to-nature enzymatic processes -- 1.5 Enzymes in multicatalytic systems -- 1.6 Outlook -- References -- 2 Biocatalysis and Green Chemistry: assessing the greenness of enzymatic processes -- 2.1 Introduction -- 2.2 Green Chemistry metrics -- 2.2.1 Mass-based metrics -- 2.2.2 Energy-based metrics -- 2.2.3 Environmental, health, and safety-based metrics -- 2.3 Green Chemistry in biocatalysis for practitioners: defining the boundaries of a biocatalytic reaction -- 2.3.1 Environmental metrics for a gate-to-gate biocatalytic reaction using the E-factor -- 2.3.1.1 The upstream unit -- 2.3.1.2 The downstream unit -- 2.3.1.3 The gate-to-gate overall environmental impact -- 2.3.1.4 The ultimate fate of the wastes: the total carbon dioxide release -- 2.4 Conclusions -- References -- 3 Study of stereocontrol in enzymatic reactions using atomic models and computational methods -- 3.1 Introduction -- 3.2 Relevant features for stereocontrol in enzymes -- 3.2.1 Noncovalent interactions at the active site -- 3.2.2 Gating and access/leaving channels for substrates and products -- 3.2.3 The role of dynamics in enzyme catalysis -- 3.3 Studying the stereocontrol in enzyme catalysis using atomic models.
3.3.1 STEP 1: access to an atomic enzyme-substrate complex model -- 3.3.1.1 Atomic structure of the enzyme -- 3.3.1.2 Atomic structure of the substrate -- 3.3.1.3 Atomic model of the enzyme-substrate complex -- 3.3.2 STEP 2: refinement of the enzyme-substrate complex -- 3.3.3 STEP 3: simulation of the chemical steps of the enzymatic reaction using atomic ES complex models -- 3.3.3.1 Cluster method and quantum mechanics/molecular mechanics scheme -- 3.3.3.2 Definition of quantum mechanics region -- 3.3.3.3 Computation of energy barrier of enzyme-catalyzed reactions -- 3.3.4 STEP 4: unveiling of the stereocontrol in enzymatic reactions and rationalization of experimental data -- 3.3.4.1 Reproduction and comparison with experimental values -- 3.4 Some final considerations for a step-by-step protocol for simulation of enzyme activity -- 3.4.1 Note of the authors -- References -- 4 Control of the activity and enantioselectivity in biocatalyzed procedures: immobilization, medium engineering, and protei... -- 4.1 Introduction -- 4.2 Immobilization of enzymes -- 4.2.1 Preface -- 4.2.2 Examples of enzyme immobilization and synthetic application -- 4.2.2.1 Enzyme immobilization through organic-inorganic nanocrystal formation -- 4.2.2.2 Enzyme immobilization on/in metal-organic frameworks -- 4.3 Medium engineering -- 4.3.1 Preface -- 4.3.2 Advantages and disadvantages of medium engineering in enantioselective synthesis -- 4.3.3 Nonaqueous media used for biocatalysis -- 4.3.4 Examples of enantioselective synthesis in nonaqueous media -- 4.3.4.1 Examples of enantioselective synthesis in organic solvents -- 4.3.4.2 Examples of enantioselective synthesis employing pressurized gas -- 4.3.4.3 Examples of enantioselective synthesis in room-temperature ionic liquids -- 4.4 Protein engineering -- 4.4.1 Preface.
4.4.2 Examples of controlling the activity and enantioselectivity by (semi)-rational design -- 4.4.3 Examples of controlling the activity and enantioselectivity by directed evolution -- 4.4.4 Factors for controlling the activity and enantioselectivity of alcohol dehydrogenases -- 4.5 Conclusions and future perspectives -- References -- 5 Hydrolases and their application in asymmetric synthesis -- 5.1 Hydrolases -- 5.1.1 Hydrolase classification and market -- 5.1.2 Structural features of serine hydrolases -- 5.1.2.1 Structural features of lipases -- 5.1.2.2 Protease structural classification -- 5.1.3 Reactions and catalytic mechanism of hydrolases -- 5.2 Low/nonaqueous solvents as media for asymmetric synthesis by hydrolases -- 5.2.1 Classical organic solvents -- 5.2.2 Neoteric solvents -- 5.2.2.1 Ionic liquids -- 5.2.2.2 Deep eutectic solvents -- 5.2.2.3 Supercritical and pressurized solvents -- 5.2.2.4 Biobased and ecofriendly solvents -- 5.3 Asymmetric synthesis catalyzed by key lipases -- 5.3.1 Candida antarctica lipase B -- 5.3.2 Lipase from Pseudomonas cepacia -- 5.3.3 Other microbial lipases -- 5.3.3.1 Candida rugosa lipases -- 5.3.3.2 Candida antarctica lipase A -- 5.3.3.3 Pseudomonas fluorescens lipase -- 5.3.3.4 Thermomyces lanuginosus lipase -- 5.3.4 Plant and animal lipases -- 5.3.4.1 Carica papaya lipase -- 5.3.4.2 Porcine lipases -- 5.4 Proteases (peptidases) -- 5.5 Other hydrolases in asymmetric synthesis -- 5.6 Tools to discover and improve hydrolases -- 5.6.1 Screening of new hydrolases -- 5.6.2 Directed and rational genetic engineering -- 5.7 Conclusions -- References -- 6 Biocatalysis for the selective reduction of carbonyl groups -- 6.1 Introduction -- 6.1.1 Alcohol dehydrogenases properties -- 6.1.2 Use of alcohol dehydrogenases in nonconventional media.
8.4 Perspectives and concluding remarks -- References -- 9 Synthesis of chiral compounds through biooxidations -- 9.1 Introduction -- 9.2 Dehydrogenases -- 9.3 Oxidases -- 9.4 Peroxidases -- 9.5 Monooxygenases -- 9.5.1 Flavoprotein monooxygenases -- 9.5.2 Cytochrome P450 monooxygenases -- 9.5.3 Opportunities and challenges employing monooxygenases -- 9.6 Peroxygenases -- 9.7 Conclusion and perspectives -- References -- 10 Asymmetric biocatalysis in nonconventional media: neat conditions, eutectic solvents, and supercritical conditions -- 10.1 Introduction -- 10.2 Neat conditions -- 10.2.1 Hydrolase-mediated various asymmetric catalysis -- 10.2.2 Oxidoreductase-mediated asymmetric redox catalysis -- 10.2.3 Transaminases-catalyzed asymmetric synthesis of chiral amines -- 10.2.4 Lyases and hydrolases for asymmetric aldol reactions -- 10.2.5 Biocatalyst-involved asymmetric cascades -- 10.3 Eutectic solvents -- 10.3.1 Introduction of deep eutectic solvents -- 10.3.2 Hydrolase-catalyzed asymmetric catalysis in DESs -- 10.3.3 Redox asymmetric catalysis in deep eutectic solvents -- 10.3.4 Other asymmetric catalysis in deep eutectic solvents -- 10.3.5 The latest trend of biocatalysis in deep eutectic solvents -- 10.4 Supercritical conditions -- 10.4.1 An overview on supercritical fluids -- 10.4.2 Hydrolase-catalyzed asymmetric catalysis in SCFs -- 10.4.3 Redox and the other asymmetric catalysis in supercritical fluids -- 10.5 Summary and perspectives -- References -- 11 Multienzyme-catalyzed processes in asymmetric synthesis: state of the art and future trends -- 11.1 Introduction -- 11.1.1 Definition and classification of multienzyme-catalyzed processes -- 11.1.1.1 Simultaneous mode -- 11.1.1.2 Sequential mode -- 11.1.2 History -- 11.1.3 Advantages and challenges of multienzyme-catalyzed processes in asymmetric synthesis.
edited by Gonzalo De Gonzalo and Andřs R. Alcántara.