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  • 1
    Online-Ressource
    Online-Ressource
    Newark :John Wiley & Sons, Incorporated,
    Schlagwort(e): Biotechnology -- Industrial applications. ; Electronic books.
    Materialart: Online-Ressource
    Seiten: 1 online resource (259 pages)
    Ausgabe: 1st ed.
    ISBN: 9783527623396
    Sprache: Englisch
    Anmerkung: Intro -- Multi-Step Enzyme Catalysis -- Contents -- Preface -- List of Contributors -- 1 Asymmetric Transformations by Coupled Enzyme and Metal Catalysis: Dynamic Kinetic Resolution -- 1.1 Introduction -- 1.2 Some Fundamentals for DKR -- 1.2.1 Enzymes for Kinetic Resolution -- 1.2.2 Metal Catalysts for Racemization -- 1.2.3 Enzyme-Metal Combination for DKR -- 1.2.4 (R)- and (S)-Selective DKR -- 1.3 Examples of DKR -- 1.3.1 First DKR of Secondary Alcohols -- 1.3.2 DKR of Secondary Alcohols with Racemization Catalyst 1 -- 1.3.3 DKR of Secondary Alcohols with Racemization Catalyst 2 -- 1.3.4 DKR of Secondary Alcohols with Racemization Catalyst 3 -- 1.3.5 DKR of Secondary Alcohols with Racemization Catalyst 4 -- 1.3.6 DKR of Secondary Alcohols with Racemization Catalyst 5 -- 1.3.7 DKR of Secondary Alcohols with Racemization Catalyst 6 -- 1.3.8 DKR of Secondary Alcohols with Racemization Catalyst 7 -- 1.3.9 DKR of Secondary Alcohols with Air-Stable Racemization Catalysts -- 1.3.10 DKR of Secondary Alcohols with Racemization Catalyst 10 -- 1.3.11 DKR of Secondary Alcohols with Aluminum Catalysts -- 1.3.12 DKR of Secondary Alcohols with Vanadium Catalysts -- 1.4 Conclusions -- References -- 2 Chemoenzymatic Routes to Enantiomerically Pure Amino Acids and Amines -- 2.1 Introduction -- 2.2 Amino Acids -- 2.3 Amines -- References -- 3 Oxidizing Enzymes in Multi-Step Biotransformation Processes -- 3.1 Oxidizing Enzymes in Biocatalysis -- 3.2 Classes of Oxidizing Enzymes -- 3.3 Mechanisms of Biological Oxidation and Implications for Multi-Enzyme Biocatalysis -- 3.4 Multi-Step Biotransformation Processes Involving Oxidation -- 3.5 Design and Development of New Multi-Enzyme Oxidizing Processes -- 3.5.1 Coupling Redox Enzymes -- 3.5.2 Cofactor Recycle in Multi-Step Oxidizing Biocatalytic Systems. , 3.6 Examples of Multi-Enzyme Biotransformation Processes Involving Oxidizing Enzymes -- 3.6.1 Coupling of Oxidases with Non-Redox Enzymes -- 3.6.2 Biocatalytic Systems Involving Coupled Oxidizing Enzymes -- 3.7 Multi-Enzyme Systems in Whole-Cell Biotransformations and Expression of Redox Systems in Recombinant Hosts -- 3.8 Other Applications of Multi-Enzyme Oxidizing Systems -- 3.9 Conclusions -- References -- 4 Dihydroxyacetone Phosphate-Dependent Aldolases in the Core of Multi-Step Processes -- 4.1 Introduction -- 4.2 DHAP-Dependent Aldolases -- 4.2.1 Problem of DHAP Dependence -- 4.2.2 DHAP-Dependent Aldolases in the Core of Aza Sugar Synthesis -- 4.2.3 Combined Use of Aldolases and Isomerases for the Synthesis of Natural and Unnatural Sugars -- 4.2.4 DHAP-Dependent Aldolases in the Synthesis of Natural Products -- 4.3 Fructose-6-Phosphate Aldolase: An Alternative to DHAP-Dependent Aldolases? -- 4.4 Conclusions -- References -- 5 Multi-Enzyme Systems for the Synthesis of Glycoconjugates -- 5.1 Introduction -- 5.2 In Vitro and In Vivo Multi-Enzyme Systems -- 5.3 Combinatorial Biocatalysis -- 5.3.1 Synthesis and In Situ Regeneration of Nucleotide Sugars -- 5.3.2 Synthesis of Oligosaccharides, Glycopeptides and Glycolipids Oligosaccharides -- 5.4 Combinatorial Biosynthesis -- 5.4.1 Synthesis of Oligosaccharides with Metabolically Engineered Cells -- 5.5 Conclusions -- References -- 6 Enzyme-Catalyzed Cascade Reactions -- 6.1 Introduction -- 6.2 Enzyme Immobilization -- 6.3 Reaction Types: General Considerations -- 6.4 Chiral Alcohols -- 6.5 Chiral Amines -- 6.6 Chiral Carboxylic Acid Derivatives -- 6.7 C-C Bond Formation: Aldolases -- 6.8 Oxidations with O(2) and H(2)O(2) -- 6.9 Conclusions and Prospects -- References -- 7 Multi-modular Synthases as Tools of the Synthetic Chemist -- 7.1 Introduction -- 7.2 Excised Domains for Chemical Transformations. , 7.2.1 Function of Individual Domains and Domain Autonomy -- 7.2.2 Heterocyclization and Aromatization -- 7.2.3 Macrocyclization -- 7.2.4 Halogenation -- 7.2.5 Glycosylation -- 7.2.6 Methyltransferases -- 7.2.7 Oxidation -- 7.3 Conclusions -- References -- 8 Modifying the Glycosylation Pattern in Actinomycetes by Combinatorial Biosynthesis -- 8.1 Bioactive Natural Products in Actinomycetes -- 8.2 Deoxy Sugar Biosynthesis and Gene Clusters -- 8.3 Characterization of Sugar Biosynthesis Enzymes -- 8.4 Strategies for the Generation of Novel Glycosylated Derivatives -- 8.4.1 Gene Inactivation -- 8.4.2 Gene Expression -- 8.4.3 Combining Gene Inactivation and Gene Expression -- 8.4.4 Endowing a Host with the Capability of Synthesizing Different Sugars -- 8.5 Generation of Glycosylated Derivatives of Bioactive Compounds -- 8.5.1 Macrolides -- 8.5.2 Aureolic Acid Group -- 8.5.3 Angucyclines -- 8.5.4 Anthracyclines -- 8.5.5 Indolocarbazoles -- 8.5.6 Aminocoumarins -- References -- 9 Microbial Production of DNA Building Blocks -- 9.1 Introduction -- 9.2 Screening of Acetaldehyde-Tolerant Deoxyriboaldolase and Its Application for DR5P Synthesis -- 9.3 Construction of Deoxyriboaldolase-Overexpressing E. coli and Metabolic Analysis of the E. coli Transformants for DR5P Production from Glucose and Acetaldehyde -- 9.4 Efficient Production of DR5P from Glucose and Acetaldehyde by Coupling of the Alcoholic Fermentation System of Baker's Yeast and Deoxyriboaldolase-Expressing E. coli -- 9.5 Biochemical Retrosynthesis of 2'-Deoxyribonucleosides from Glucose Acetaldehyde and a Nucleobase: Three-Step Multi-Enzyme-Catalyzed Synthesis -- 9.6 One-Pot Multi-Step Enzymatic Synthesis of 2'-Deoxyribonucleoside from Glucose, Acetaldehyde and a Nucleobase. , 9.7 Improvement of the One-Pot Multi-Step Enzymatic Process for Practical Production of 2'-Deoxyribonucleoside from Glucose, Acetaldehyde and a Nucleobase -- 9.8 Conclusions -- References -- 10 Combination of Biocatalysis and Chemical Catalysis for the Preparation of Pharmaceuticals Through Multi-Step Syntheses -- 10.1 Introduction: Biocatalysis and Chemical Catalysis -- 10.2 Pharmaceuticals with Hydrolases -- 10.2.1 Enzymatic Hydrolysis -- 10.2.2 Enzymatic Transesterification -- 10.2.3 Enzymatic Aminolysis -- 10.3 Pharmaceuticals with Oxidoreductases -- 10.4 Pharmaceuticals with Lyases -- 10.5 Conclusions -- References -- Index.
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  • 2
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    The @journal of organic chemistry 60 (1995), S. 7360-7363 
    ISSN: 1520-6904
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 3
    ISSN: 1520-6904
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    The @journal of organic chemistry 60 (1995), S. 4294-4295 
    ISSN: 1520-6904
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    Journal of the American Chemical Society 117 (1995), S. 8031-8032 
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 6
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
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  • 7
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
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  • 8
    Digitale Medien
    Digitale Medien
    Springer
    Plant cell reports 5 (1986), S. 155-157 
    ISSN: 1432-203X
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Mixed cells of Pseudevennia Lun-Lunacea thallus have been entrapped in polyacrylamide gel and used in a continuous column process to hydrolyze evernic acid. Equimolar amounts of both orsellinic and everninic acids are recovered. The activity of entrapped cells, which contain orsellinate depside hydrolase, is unaltered over a period of two months.
    Materialart: Digitale Medien
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  • 9
    ISSN: 0887-3585
    Schlagwort(e): aldolase ; protein complex crystallization ; crystallization screening ; X-ray crystallography ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: X-ray quality crystals of class I deoxyribose-5-phosphate aldolase from Escherichia coli have been obtained for the unliganded enzyme and in complex with its substrate, 2-deoxyribose-5-phosphate. The enzyme catalyzes the reversible cleavage of 2-deoxyribose-5-phosphate to acetaldehyde and D-glyceraldehyde-3-phosphate. The unliganded and complex crystals are prismatic long rods and belong to the orthorhombic space group P212121 with cell dimensions a = 183.1 Å, b = 61.4 Å, c = 49.3 Å and a = 179.2 Å, b = 60.5, Å, c = 49.1 Å, respectively. Two molecules in the asymmetric unit are related by a noncrystallo-graphic 2-fold axis. The crystals are stable in the X-ray beam and diffract to at least 2.6 Å. A new method, reverse screening, designed to minimize protein utilization during the screening process was used to determine supersaturation and crystallization conditions. © 1995 Wiley-Liss, Inc.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
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