— Contents.- Special Methods of Isolation and Purification.- Enzymes du Métabolisme du Soufre.- A. Enzymes d’activation et de transfert du sulfate.- I. Enzymes d’activation du sulfate.- 1. Mesure de l’activité enzymatique.- a) Système complet d’activation.- b) ATP-sulfurylase — Robbins et Lipmann (1958a).- c) ADP-sulfurylase — Robbins et Lipmann (1958a).- d) APS-kinase — Robbins et Lipmann (1958a).- 2. Préparation de l’ATP-sulfurylase, de l’ADP-sulfurylase et de l’APS-kinase.- II. Enzymes de transfert du sulfate.- 1. Mesure de l’activité de la phénol-sulfokinase.- 2. Préparation de la phénol-sulfokinase — Gregory et Lipmann (1957) . ..- B. Systèmes réducteurs du sulfate.- 1. Mesure de l’activité sulfato-réductrice.- 2. Préparation du système réducteur du sulfate, Hilz, Kittler et Knape (1959).- C. Sulfatases.- 1. Arylsulfatases.- Préparation des arylsulfatases.- 2. Chondrosulfatases.- 3. Myrosulfatases.- 4. Glucosulfatases.- 5. Stéroïdesulfatases.- 6. Cholinesulfatase.- D. Enzymes du métabolisme du thiosulfate, du sulfite et du sulfure.- I. Enzymes du métabolisme du thiosulfate.- 1. Thiosulfate-réductase.- 2. Rhodanèse.- II. Enzymes du métabolisme du sulfite.- 1. Formation du sulfite par désulfination.- 2. Sulfite-réductase.- 3. Sulfite-oxydase.- III. Enzymes du métabolisme du sulfure.- 1. Formation d’hydrogène sulfuré à partir de la cystéine.- 2. Sérine-sulfhydrase.- 3. Oxydation du sulfure.- Bibliographie.- Enzymes of Phosphate Metabolism.- I. Special Features of Enzyme Isolation and Purification.- 1. Choice of Starting Material.- 2. Conventional versus Modern Methods of Enzyme Purification.- a) Automatic Device for Ammonium Sulfate Addition.- b) Dialysis of Enzyme Solutions.- 3. Stability of Enzymes on Dilution.- II. Assay of Phosphatase Activity.- 1. Colorimetric Estimation of Phosphorus.- 2. Aspects of Enzyme Assay in Plants and Microorganisms.- III. Intracellular Localization of Enzymes by the Technique of Differential Centrifugation.- 1. Nuclear Fraction.- 2. Plastid Fraction.- 3. Mitochondrial Fraction.- 4. Cell Wall Fraction.- 5. Association of Enzymes with Larger Particles.- 6. Isolation of Plant Protoplasts.- 7. Localization of Phosphatases.- IV. Phosphatases Acting on Hexose Phosphates.- 1. The Hydrolysis of Glucose-1-Phosphate.- 2. C1 Diphosphatases.- a) Fructose Diphosphatase.- b) Fructose Diphosphatase of Animal Tissue.- c) Fructose Diphosphatase of Plants.- d) Neutral Fructose Diphosphatase.- e) Acidic Fructose Diphosphatase.- f) Acid C1 Diphosphatase of Escherichia coli.- g) Role of Alkaline Fructose Diphosphatase in Green Plants.- 3. Sedoheptulose-1,7 -Diphosphatase.- 4. Glycerate-2,3-Diphosphatase.- V. Enzymes Acting on Condensed Phosphates.- 1. Inorganic Pyrophosphatases.- a) Inorganic Pyrophosphatase of Microorganisms.- b) Inorganic Pyrophosphatases of Animal Tissue.- 2. Tripolyphosphatases.- 3. Tetrapolyphosphatases.- 4. Trimetaphosphatases.- 5. Tetrametaphosphatases.- VI. Enzymes Acting on Polyphosphates.- Type I Enzyme: Polyphosphate Depolymerases.- Type II Enzyme: Polyphosphatases.- a) Type I.- b) Type II.- c) Type III.- Type III Enzyme: Enzymes Transfering Phosphate Groups from Polyphosphates to Suitable Acceptors.- Polyphosphate-ADP-phosphotransferase of Escherichia coli.- VII. General Phosphomonoesterases.- 1. Acid Phosphatases.- 2. Alkaline Phosphatases.- a) Alkaline Phosphatases of Microorganisms.- VIII. Phosphoprotein Phosphatase.- IX. Ortho Phosphoserine Phosphatase.- X. Phosphatase Acting on Nucleotides and Nucleic Acids.- 1. Nucleotide Pyrophosphatases.- a) Nucleotide Pyrophosphatase of Potato.- b) Nucleotide Pyrophosphatase of Tobacco.- 2. 5’-Nucleotidases.- a) 5’-Nucleotidase of Clostridium stricklandii.- 3. Ribonucleases.- a) Ribonucleases of Plants.- b) Endonucleases from Microorganisms.- c) Phosphodiesterases Acting on Polynucleotides.- References.- Enzymes of Inorganic Nitrogen Metabolism.- A. Nitrate Reductase.- I. Preparation.- 1. Fungi and Higher Plants.- 2. Bacteria.- a) Methods of extraction.- b) Fractionation and Stability.- II. Measurement of Activity.- 1. Assay Methods.- 2. Sources of Error.- III. Electron Donors and Co-Factors.- 1. Fungi and Higher Plants.- a) Pyridine nucleotides and other electron donors.- b) Flavins.- c) Metal and Anion Requirements.- 2. Bacteria.- IV. Properties and Mechanisms.- 1. Fungi and Higher Plants.- 2. Bacteria.- V. Physiological Factors.- 1. Fungi and Higher Plants.- 2. Bacteria.- B. Other Nitrate Reduction and Nitro Reductase Enzymes.- 1. Aldehyde and Xanthine Oxidases of Animal Origin.- 2. Aldehyde Oxidase of Potato.- 3. Reduction of Aromatic Nitro-Compounds.- C. Nitrite, Nitric Oxide, Hyponitrite and Hydroxylamine Reductases and Related Enzymes.- I. Preparation.- 1. Fungi and Higher Plants.- 2. Bacteria.- II. Fractionation and Stability.- III. Measurement of Activity.- 1. Interference and Errors.- 2. Assay Methods.- a) Use of CONWAY Methods for NH3 Determinations.- b) Hydroxylamine.- c) Oximes, YAMAFUJI and AKITA (1952).- d) Hyponitrite.- e) Assay Methods Using Reduced Benzyl Viologen and Other Dyes under Anaerobic Conditions.- f) Manometric Assay of Nitrite Reductase.- g) Manometric Assay of Nitric Oxide Reductase.- 3. Preparation of Hyponitrite as a Substrate.- IV. Electron Donors and Co-Factors and Inhibitors.- 1. Fungi and Higher Plants.- a) Nitrite Reductase.- b) Hyponitrite Reductase.- c) Hydroxylamine Reductase.- 2. Bacteria.- a) Nitrite Reductase.- b) Nitric Oxide Reductase.- c) Hydroxylamine Reductase.- V. Properties and Mechanisms.- 1. Fungi and Higher Plants.- 2. Bacteria.- a) Nitrite Reductase.- b) Nitric Oxide Reductase.- c) Hydroxylamine Reductase.- VI. Physiological Factors and Other Features.- 1. Fungi and Higher Plants.- a) Nitrite Reductase.- b) Hydroxylamine Reductase.- D. Glutamic Dehydrogenase.- E. Oxidation and Other Reactions of Ammonia, Hydroxylamine and Nitrite.- I. Fungi and Higher Plants.- Hydroxylamine “Oxidase” of Higher Plants.- II. Bacteria (Enzymes of Nitrification).- 1. Preparation.- 2. Measurement of Activity.- 3. Cofactors.- 4. Properties and Mechanisms.- Reversal of NH2OH reductase “Ammonia dehydrogenase” artefact.- Literature.- Enzymes of Vitamin Metabolism.- A. Enzymes Concerned with Biosynthesis.- 1. Thiamine.- a) General Preparation of Enzyme Fractions.- b) Pyrimidine Kinase.- c) Thiazole Kinase.- d) Thiamine Phosphate Synthetase..- e) Thiamine Phosphatase.- 2. Riboflavin.- 3. Nicotinic Acid.- a) Tryptophan Pyrrolase.- b) Formylase (Kynurenine Formamidase).- c) Kynurenine Hydroxylase.- d) Kynureninase.- 4. Folic Acid.- 5. Pantothenic Acid.- Pantothenate Synthetase.- B. Activating Enzymes.- 1. Thiamine.- a) Thiamine Pyrophosphokinase.- b) Thiamine Pyrophosphate Kinase.- 2. Riboflavin.- a) Flavokinase.- b) FAD Pyrophosphorylase.- 3. Pyridoxal (Vitamin B6).- Pyridoxal Phosphokinase.- 4. Nicotinic Acid.- a) PRPP-Nicotinic Acid Transferase.- b) DPN-Pyrophosphorylase.- c) DPN-Synthetase.- d) DPN-Kinase.- 5. Folic Acid.- a) Folic Acid Reductase.- b) Dihydrofolic Acid Reductase.- 6. Pantothenic Acid.- a) Pantothenate Kinase.- b) Coupling Enzyme.- c) Phosphopantothenylcysteine Decarboxylase.- d) Dephospho-CoA Pyrophosphorylase.- e) Phosphotransacetylase.- f) Dephospho-CoA Kinase.- C. Degrading Enzymes.- 1. Thiamine.- a) Thiaminase.- b) Thiamine Phosphatase.- c) Thiamine Pyrophosphatase.- 2. Riboflavin.- a) FAD-ase (Nucleotide Pyrophosphatase).- b) FMN-Phosphatase.- 3. Nicotinic Acid.- a) Nucleotide Pyrophosphatase.- b) DPN-ase (Pyridine Transglycosidase).- c) NMN-Phosphatase.- 4. Folic Acid.- 5. Pantothenic Acid.- a) “CoA-3’-Nucleotidase”.- b) “CoA Pyrophosphatase”.- c) “CoA-Peptidase”.- 6. Biotin.- d-Biotin Oxidase.- 7. Inositol.- Phytase.- 8. Carotene.- Carotene Oxidase (Lipoxidase).- References.- Enzyme des L-Ascorbinsäure-Stoflwechsels.- I. Enzyme bei der Biosynthese der L-Ascorbinsäure.- 1. Indirekte Umwandlung.- a) Aldolkondensation.- b) Acyloin-Reaktion.- 2. Direkte Umwandlung.- a) L-Galaktonsäure-?-laktondehydrogenase.- b) Enzympräparat nach Mapson U. Isherwood (1958).- c) Enzympräparat nach Nakatani.- d) L-Gulonsäuredehydrogenase nach Ishikawa U. Noguchi (1957).- e) Herstellung der gereinigten Laktonase I.- II. L-Ascorbinsäure oxydierende Enzymsysteme.- 1. Peroxydase.- 2. Cytochrom c — Cytochromoxydase.- 3. Polyphenoloxydase.- 4. Laccase.- 5. Ascorbinsäureoxydase.- a) Methoden der Kupferbestimmung.- b) Eigenschaften der AS-Oxydase.- c) Gewinnung der Ascorbinsäure-Oxydase.- d) Aktivitätsbestimmungen der AS-Oxydase.- e) Vorkommen der AS-Oxydase.- 6. Andere Ascorbinsäure oxydierende Enzyme.- III. L-Ascorbinsäure reduzierende Enzymsysteme.- 1. Herstellung des gereinigten Enzympräparates nach Janecke U. Ragab.- 2. Darstellung der L-Dehydroascorbinsäure.- 3. Verbreitung der DAS-Reduktase.- Literatur.- Enzymes Involved in the Synthesis and Breakdown of Indoleacetic Acid.- I. General Methods.- Separations of IAA from its Precursors in the Reaction Mixture.- II. Enzymes Involved in the Synthesis of IAA.- 1. Enzymes Involved in the Conversion of TTP to IAA.- a) Distribution.- b) Pathways for the Conversion of TTP to IAA.- c) Conversion of IPyA to IAc and IAA.- d) Preparation and Properties of Some Enzymes Converting TTP to IAA.- 2. Enzymes Involved in the Conversion of IAc to IAA.- Preparation of the Enzym es.- 3. Enzymes Involved in the Conversion of TNH2 to IAc and IAA.- 4. Enzymes Involved in the Conversion of IAN to IAA.- III. Enzymes Involved in the Breakdown of IAA.- 1. General Properties of the IAA Oxidation Reaction.- 2. Preparation and Properties of some IAA Oxidases.- a) Lupin Enzyme.- b) Pea Enzyme.- c) Wheat Leaf Enzyme.- d) Pineapple Enzyme.- e) Omphalia Enzyme.- References.- Enzymes of Aromatic Biosynthesis.- I. Enzymes of Aromatic Biosynthesis from Non-Aromatic Compounds in Microorganisms.- a) 2-Keto-3-Deoxy-D-Araboheptonic Acid-7-Phosphate (KDHP) Synthetase.- b) The Enzyme Converting KDHP to Dehydroquinate.- c) Dehydroshikimic (DHS) Dehydrase.- d) 5-Dehydroquinase.- e) Quinic Dehydrogenase.- f) 5-Dehydroshikimic Reductase.- g) ATP-Shikimic Acid Transphosphorylase.- h) The Enzymes Forming 3-Enolpyruvyl Shikimate-5-Phosphate (ESP) from 5-Phosphoshikimic Acid and Phosphoenolpyruvate.- i) Prephenic Aromatase.- k) Prephenic Dehydrogenase.- II. The Shikimic Acid Pathway in Higher Plants.- III. Conversion of Simple Phenylpropanoids to Lignin and Related Compounds.- a) Tyrase.- b) Phenylalanine deaminase.- IV. Conversion of Coniferin and Coniferyl Alcohol to Coniferous Lignin.- 1. Dehydrogenation of Coniferyl Alcohol by Laccase and Peroxidase.- a) Mushroom Enzyme.- b) The Enzyme of Spruce Cambial Sap.- c) The Enzyme of Japanese Lacquer.- 2. Coupled Oxidation of Coniferyl Alcohol by Yellow Enzyme-Peroxidase Systems.- References.- Enzymes of Amino Acid Metabolism..- 1. Enzymes of Deamination, Decarboxylation, Transmethylation and Intermediary Metabolism.- A. Enzymes of Oxidative Deamination.- I. Pyridine Nucleotide linked Dehydrogenases.- 1. L-Glutamic Dehydrogenase of Higher Plants.- 2. L-Glutamic Acid Dehydrogenase of Neurospora and Other Microorganisms.- 3. L-Alanine Dehydrogenase.- 4. L-Leucine Dehydrogenase.- II. D- and L-Amino Acid Oxidases.- 1. D-Amino Acid Oxidase of Microorganisms.- 2. D-Glutamic Acid Oxidase.- 3. L-Amino Acid Oxidase of Microorganisms.- III. Amine Oxidases.- Amine Oxidase of Pea Seedlings.- B. Enzymes of Amino Acid Decarboxylation.- I. Amino Acid Decarboxylases of Higher Plants.- Glutamic Decarboxylase.- II. Amino Acid Decarboxylases of Microorganisms.- 1. Glutamic Acid Decarboxylase of Escherichia coli.- 2. Lysine Decarboxylase of E. coli.- 3. Arginine Decarboxylase of E. coli.- 4. Leucine Decarboxylase.- 5. L-Trytophan Decarboxylase.- 6. Diaminopimelic Acid Decarboxylase.- 7. Tyrosine Decarboxylase..- C. Enzymes of Non-Oxidative Deamination.- I. Amino Acid Deaminases.- 1. Aspartase.- 2. Histidase.- II. Dehydrative Deaminases.- 1. Dehydrases.- a) L-Threonine (and L-Serine) Dehydrase.- b) D-Serine (and D-Threonine) Dehydrase.- 2. Desulfhydrases.- a) L-Cysteine Desulfhydrase.- b) D-Cysteine Desulfhydrase.- c) Homocysteine Desulfhydrase.- III. Amino Acid C—S Cleaving Enzymes.- 1. Methionine Dethiomethylase.- 2. Dimethylpropionthetin Dethiomethylase.- 3. Cystathionase.- 4. Alliinase.- 5. C—S-Lyase.- IV. Amino Acid Reductases.- 1. Proline Reductase.- 2. Glycine Reductase System.- D. Enzymes of Transmethylation.- I. Enzymes of Metabolism of S-Adenosylmethionine and Thetins.- 1. Methionine Activating Enzyme.- 2. Cleavage of S-Adenosylmethionine.- 3. S-Methylmethionine-Homocysteine Transmethylase.- 4. Adenosylmethionine-Homocysteine Transmethylase.- 5. Adenosylmethionine-Nicotinic Acid Transmethylase (Nicotinic Acid Methylpherase).- E. Enzymes of Biosynthesis.- I. Enzymes of L-Threonine Biosynthesis.- 1. ?-Aspartokinase.- 2. Aspartic ?-Semialdehyde Dehydrogenase.- 3. Homoserine Dehydrogenase.- 4. L-Homoserine Kinase.- 5. Threonine Synthetase (Homoserine Phosphate Mutaphosphatase).- II. Enzymes of L-Histidine Biosynthesis.- 1. Imidazoleglycerol Phosphate Dehydrase.- 2. Imidazoleacetol Phosphate Transaminase.- 3. L-Histidinol Phosphate Phosphatase.- 4. L-Histidinol Dehydrogenase.- III. Enzymes of L-Proline Biosynthesis.- ?’-Pyrroline-5-Carboxylate Reductase.- IV. Enzymes of Ornithine Synthesis.- 1. Higher Plants, Molds and Animals.- Ornithine ?-transaminase.- 2. Escherichia coli.- a) Amino Acid Transacetylase.- b) Acetylornithine ?-Transaminase.- c) Acetylornithinase.- V. Enzymes of the Urea Cycle and Related Compounds (synthetic).- 1. Carbamyl Phosphate Synthesizing Enzymes.- 2. Carbamate Kinase.- 3. Ornithine Transcarbamylase.- 4. Argininosuccinate Synthetase.- 5. Argininosuccinase.- 6. Arginase.- VI. Enzymes of Arginine Degradation.- 1. Arginine Desiminase.- 2. Citrullinase System (Citrulline Ureidase).- VII. Enzymes of Synthesis of Branched-chain Amino Acids (Leucine, Isoleucine, Valine).- 1. Acetolactate Synthetase (Acetolactate Forming Enzyme).- 2. ?-Hydroxy- ?-keto Acid Reductoisomerase.- 3. ?, ?-Dihydroxy Acid Dehydrase.- 4. Branched-Chain Amino Acid Transaminase.- VIII. Degradation of the Branched Chain Amino Acids.- IX. Formation of Succinic Acid from Glutamic Acid.- 1. Succinic Semialdehyde Dehydrogenases.- 2. ?-Hydroxybutyrate Dehydrogenase.- X. Enzymes of Synthesis of Glycine and Serine.- 1. 3-Phosphoglycerate ? Serine.- 2. Formate ? Serine.- a) Hydroxymethyltetrahydrofolate Dehydrogenase.- b) Serine Aldolase (Serine Transhydroxymethylase).- 3. Glycoldehyde ? Glycine.- XI. Enzymes of Synthesis of Tryptophan.- 1. Indole-3-Glycerol Phosphate Synthetase.- 2. Tryptophan Synthetase.- References.- 2: Transaminases and Racemases.- A. Transaminases.- I. D-Amino Acid Transaminases.- II. L-Ammo Acid Transaminases.- 1. Glutamate-Aspartate Transaminase.- a) Assay of Glutamate-Aspartate Transaminase.- b) Purification of the Enzyme from Plants.- c) Properties of the Plant Enzyme.- 2. Glutamate-Alanine Transaminase.- 3. Cysternesulfinate Transaminase.- 4. ?-Alanine (?-Aminoisobutyrate)-Glutamate Transaminase.- 5. ?-Alanine-Glycine Transaminase.- 6. ?-Alanine-?-Alanine Transaminase.- 7. ?-Aminobutyrate-Glutamate Transaminase.- 8. Kynurenine Transaminase.- 9. Glutamate-Phosphohistidinol Transaminase.- 10. Ornithine Transaminase.- 11. Serine-Alanine Transaminase.- 12. Tyrosine-Glutamate Transaminase.- 13. Glutamine and Asparagine Transaminases.- 14. Alanine, Phenylalanine, Glutamate-Branched Cham Amino Acids.- 15. Other Transaminases.- III. Transamidination.- 1. Assay.- 2. Properties.- B. Racemases.- 1. Alanine Racemase.- 2. Glutamate Racemase.- 3. Threonine Racemase.- 4. Methionine Racemase.- 5. Lysine Racemase.- 6. Proline Racemase.- 7. ?-?-Diaminopimelic Acid (DAP) Racemase.- 8. Other Amino Acid Racemases.- References.- Enzymes of Peptide and Protein Metabolism.- A. Enzymes Concerned with Syntheses (Synthetases).- I. Amide Synthesis.- 1. Glutamine Synthetase.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- 2. Asparagine Synthetase.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- II. Peptide Synthesis.- 1. Glutamylcysteine Synthetase.- a) Occurrence.- b) Assay.- c) Preparation of Glutamylcysteine Synthetase.- d) Properties.- 2. Glutathione Synthetase.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- III. Protein Synthesis.- 1. Amino Acid-Activating Enzymes.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- 2. Enzymes Concerned with Protein Synthesis.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- B. Enzymes concerned with Degradation (Amidases, Peptidases and Proteases).- I. Amidases.- Glutaminase and Asparaginase.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- II. Peptidases.- a) Occurrence.- b) Assay.- c) Preparation and Properties.- III. Proteases.- a) Occurrence.- b) Assay.- c) Preparation.- d) Properties.- References.- Enzymes of Synthesis of Purine and Pyrimidine Nucleotides.- A. Enzymes of Synthesis of Purine Nucleotides.- I. 5-Phosphoribosylpyrophosphate Kinase.- 1. Assay.- 2. Enzyme Preparation.- a) Procedures of KORNBERG et al. (1955).- b) Procedures of KORN et al. (1955).- II. 5-Phosphoribosylpyrophosphate Amidotransferase.- 1. Assay.- 2. Enzyme Preparations.- III. Glycinamide Ribotide Kinosynthase.- IV. Glycinamide Ribotide Transformylase.- V. Formylglycinamidine Ribotide Kinosynthase.- VI. Enzyme for the Synthesis of 5-Aminoimidazole Ribotide.- VII. 5-Aminoimidazole Ribotide Carboxylase and Enzyme for the Synthesis of 5-Amino-4-Imidazole-N-Succinocarboxamide Ribotide.- VIII. Enzymatic Cleavage of 5-Amino-4-Imidazole-N-Succinocarboxamide Ribotide (AISCAR Splitting Enzyme).- IX. 5-Amino-4-Imidazolecarboxamide Ribotide Transformylase and Inosinicase.- B. Enzymes of Synthesis of Pyrimidine Nucleotides.- I. Carbamyl Phosphate Synthetase.- II. Carbamyl Phosphate-Aspartate Transcarbamylase.- III. Dihydroorotase.- IV. Dihydroorotic Acid Dehydrogenase.- V. Orotidine-5’-Phosphate Pyrophosphorylase.- VI. Orotidine-5’-Phosphate Decarboxylase.- References.- Enzymes of Fat Metabolism.- A. Plant Lipases.- Assay Procedures.- 1. Lipase Assay by the Release of Fatty Acids.- 2. Lipase Assay by the Decrease in Ester Content.- 3. Other Assay Procedures.- 4. Activators and Inhibitors.- 5. pH Optima.- 6. Specificity of Attack.- 7. Purification.- References.- B. Phospholipases.- I. Phospholipase A.- Assay Procedure.- II. Phospholipase B (Lysophospholipase B).- Assay Procedure.- a) Estimation of Activity by Measuring the Decrease in Ester Bond.- b) Measurement of Activity by Estimating GPC Formed.- c) Other Assay Procedures.- Substrate Specificity.- pH Optima and Stability.- Activators and Inhibitors.- Purification Procedures.- III. Phospholipase C.- Assay Procedure.- Other Assay Procedures.- pH Optimum and Stability.- Activators.- Substrate Specificity.- Purification Procedures.- Purification of Cottonseed Enzyme.- IV. Phospholipase D.- Assay Procedure.- Other Assay Procedures.- pH Optima and Stability.- Activators.- Substrate Specificity.- Purification Procedure.- V. Other Enzymes Attacking Phospholipids.- 1. Phosphoinositide Phosphorylase.- 2. Phosphatidic Acid Phosphatase.- 3. Lysolecithin Isomerase.- References.- C. ?-Oxidation.- I. Even Chain Fatty Acids.- II. Odd-Chain Fatty Acids.- References.- D. ?-Oxidation.- References.- E. Lipoxidase.- 1. Assay Method.- Procedure.- a) Manometric.- b) Spectrophotometric.- 2. Purification Procedure.- 3. Properties.- References.- F. Synthesis of Fatty Acids.- 1. Preparation of Particles.- 2. Extraction of Acetone Powder.- 3. Assay.- 4. pH Optima and Stability.- References.- Enzymes of Carbohydrate Synthesis.- A. Formation of Precursors of Complex Saccharides.- I. Preparation of Substrates.- II. Separation and Identification of Reaction Products.- III. Enzymes which Catalyze the Formation of Sugar 1-Phosphates.- 1. D-Galactokinase from Saccharomyces fragilis.- 2. D-Glucuronic Acid Kinase from Phaseolus aureus.- 3. D-Galactokinase and L-Arabinokinase from Phaseolus aureus.- IV. Enzymes which Catalyze the Formation of Sugar Nucleotides.- 1. Sugar Nucleotide Pyrophosphorylases from Phaseolus aureus.- 2. UDP-D-Glucose Pyrophosphorylase from Phaseolus aureus.- 3. UDP-D-Glucose Pyrophosphorylase from Brewer’s Yeast.- 4. UDP-N-Acetyl-D-Glucosamine Pyrophosphorylase from Phaseolus aureus.- 5. UDP-N-Acetyl-D-Glucosamine Pyrophosphorylase from Baker’s Yeast.- 6. GDP-D-Mannose Pyrophosphorylase from Brewer’s Yeast.- 7. ?-D-Galactose-1-Phosphate Uridyl Transferase from Saccharomyces fragilis.- V. Enzymes which Catalyze Transformations of Sugar Nucleotides.- 1. 4-Epimerases.- a) UDP-D-Galactose 4-Epimerase from Saccharomyces fragilis.- b) 4-Epimerases from Higher Plants.- 2. UDP-D-Glucose Dehydrogenase from Peas.- 3. UDP-D-Glucuronic Acid Decarboxylase from Wheat Germ.- B. Synthesis of Disaccharides.- I. Enzymes which Catalyze the Formation of Sucrose and Sucrose Phosphate.- 1. UDP-D-Glucose-D-Fructose Transglucosylase from Wheat Germ.- 2. UDP-D-Glucose-D-Fructose 6-Phosphate Transglucosylase from Wheat Germ.- II. Enzyme which Catalyzes the Formation of Trehalose Phosphate (UDP-D-Glucose-D-Glucose 6-Phosphate Transglucosylase from Yeast).- C. Synthesis of Glycosides.- I. Enzyme which Catalyzes the Formation of Diphenol D-Glucosides (UDP-D-Glucose-Diphenol Transglucosylase from Wheat Germ).- II. Enzyme which Catalyzes the Formation of Phenolic Gentiobiosides (UDP-Glucose-Phenol-D-Glucoside Transglucosylase from Wheat Germ).- D. Synthesis of Polysaccharides.- I. Enzyme which Catalyzes the Formation of Callose.- II. Enzyme which Catalyzes the Formation of Chitin.- III. Enzyme which Catalyzes the Formation of D-Xylodextrins.- IV. Enzymes which Catalyze the Formation of Starch.- 1. Phosphorylase from Potatoes.- Procedure 1.- Procedure 2.- 2. Q-Enzyme (Branching Enzyme) from Potatoes.- 3. D-Enzyme from Potatoes.- References.- Enzymes of Glycolysis.- I. Assay of Glycolytic System.- 1. Preparation of Glycolytic System.- 2. Properties.- II. Phosphorylase.- 1. Assay Method.- 2. Purification.- 3. Properties.- III. Phosphoglucomutase.- 1. Assay Method.- 2. Preparation of Phosphoglucomutase Extracts from Plant Tissues.- 3. Properties.- IV. Hexokinase.- 1. Assay Method.- 2. Preparation of Hexokinase Extracts from Plant Tissues.- 3. Properties.- V. Phosphoglucose Isomerase.- 1. Assay Method.- 2. Preparation of Phosphoglucose Isomerase Extracts from Plant Tissues.- 3. Properties.- VI. Phosphohexokinase.- 1. Assay Method.- 2. Preparation of Phosphohexokinase from Plant Tissue.- 3. Properties.- VII. Fructose-1,6-Diphosphatase.- 1. Assay Method.- 2. Purification Procedure (Racker and Schroeder, 1958).- 3. Properties.- VIII. Aldolase.- 1. Assay Method.- 2. Purification Procedure.- 3. Properties.- IX. Triosephosphate Isomerase.- Assay Method.- X. TPN Triosephosphate Dehydrogenase.- 1. Assay Method.- 2. Purification Procedure (Gibbs, 1955).- 3. Properties.- XI. DPN Triosephosphate Dehydrogenase.- 1. Assay Method.- 2. Purification Procedure (Hageman and Arnon, 1955).- 3. Properties.- XII. Triosephosphate — Phosphoglycerate Dehydrogenase.- 1. Assay Method.- 2. Purification Procedure (Rosenberg and Arnon, 1955).- 3. Properties.- XIII. Phosphoglycerate Kinase.- 1. Assay Method.- 2. Preparation Procedure (Axelrod and BandurskI, 1953).- 3. Properties.- XIV. Phosphoglyceric Acid Mutase.- 1. Assay Method.- 2. Purification (ITO and Grisolia, 1959).- 3. Properties.- XV. Enolase, 2-Phosphoglycerate Dehydrase.- 1. Assay Method.- 2. Purification Procedure (Boser, 1959).- 3. Properties.- XVI. Pyruvate Kinase.- 1. Assay Method.- 2. Purification Procedure (Miller and Evans, 1957).- 3. Properties (Data of Miller and Evans, 1957).- References.- Enzymes of the Pentose Phosphate Cycle.- I. Hexokinase (Glucokinase and Fructokinase).- 1. Assay.- 2. Purification.- II. Glucose-6-Phosphate Dehydrogenase (Zwischenferment). Lactonase and 6-Phosphogluconic Dehydrogenase.- 1. Assay.- 2. Purification.- 3. Lactonase (Assay and Purification).- III. Phosphoriboisomerase.- 1. Assay.- 2. Purification.- 3. Preparation of Isomerase Product.- IV. Phosphoketopentoepimerase and Transketolase.- 1. Assay (Transketolase).- 2. Purification (Transketolase).- 3. Assay (Phosphoketopentoepimerase).- 4. Purification (Phosphoketopentoepimerase).- V. Transaldolase.- 1. Assay.- 2. Preparation of Sedoheptulose-7-Phosphate.- 3. Purification.- VI. Phosphohexoisomerase.- 1. Assay.- 2. Purification.- References.- Enzyme Systems in Photosynthesis.- A. The Photosynthetic Structures of Plants and Bacteria.- I. Chloroplasts.- 1. Isolation and Purification of Whole Chloroplasts.- 2. Preparation of “Broken” Chloroplasts and Chloroplast Extracts.- II. Chromatophores.- 1. Isolation and Purification of Chromatium Chromatophores.- a) Culture of Bacteria.- b) Preparation and Fractionation of Cell Extracts.- 2. Isolation and Purification of Rhodospirillum rubrum Chromatophores.- a) Culture of Bacteria.- b) Preparations of Cell-Free Extracts.- c) Preparation of Purified Chromatophores.- B. Carbon Dioxide Assimilation in Photosynthesis.- I. Separation of Light and Dark Phases in Photosynthesis.- II. Characteristic Enzymes of the Reductive Carbohydrate Cycle.- 1. Phosphoribulokinase.- a) Assay Method.- b) Purification Procedure.- c) Properties.- 2. Carboxylation Enzyme.- a) Assay Method.- b) Purification Procedure (Method of Weissbach et al., 1956).- c) Purification Procedure (Method of Jakoby et al., 1956).- d) Properties.- C. Photosynthetic Phosphorylation.- I. Cyclic Photophosphorylation.- 1. Procedure for Cyclic Photophosphorylation in Chloroplasts.- 2. Procedure for Cyclic Photophosphorylation in Chromatophores.- II. Noncyclic Photophosphorylation.- 1. Procedure for Noncyclic Photophosphorylation in Chloroplasts.- 2. Procedure for Noncyclic Photophosphorylation in Chromatophores.- D. Isolated Protein Constituents of the Photosynthetic Apparatus.- I. The TPN-Reducing System.- 1. Chloroplast Ferredoxin.- a) Isolation and Purification.- b) Crystallization of Parsley Ferredoxin.- c) Crystallization of Spinach Ferredoxin.- 2. Ferredoxin-TPN Reductase.- a) Isolation and Purification.- b) Assay Method.- c) Properties.- d) Crystallization Procedure.- II. Cytochromes in Leaves and Algae.- 1. Extraction and Purification.- a) Preparation of Cytochrome f from Parsley.- b) Crystallization of Porphyra tenera-Cytochrome 553.- 2. Properties.- III. Bacterial Cytochromes.- 1. RHP and Cytochrome c2 from R. rubrum.- a) Preparation.- b) Properties.- 2. RHP and Cytochrome c2 from Chromatium.- 3. Cytochrome-552 from Rhodopseudomonas palustris.- E. Quinone Constituents of the Photosynthetic Apparatus.- I. Extraction and Purification of Vitamin K1.- II. Extraction and Purification of Plastoquinone.- 1. Method of CRANE (1959 b).- 2. Method of BISHOP (1958, 1959).- III. Properties of Plastoquinone.- IV. Role of Quinones in Photosynthetic Reactions.- lBacterial Photophosphorylations.- V. Concluding Remarks.- References.- Enzymes of the Krebs Cycle, the Glyoxalate Cycle and Related Enzymes.- A. Enzymes of the Krebs Cycle.- I. Condensing Enzyme.- II. Aconitase.- III. Iso Citric Dehydrogenase (TPN Specific).- IV. Iso Citric Dehydrogenase (DPN Specific).- V. ?-Keto Acid Oxidases.- VI. Succinyl CoA Synthetase (P Enzyme).- VII. Succinic Dehydrogenase.- VIII. Fumarase.- IX. Malic Dehydrogenase.- E. Enzyme Activities Related to the Krebs Cycle.- I. Tartaric Dehydrogenase.- II. Malease.- III. Pyruvic (De) Carboxylase.- IV. Lactic Dehydrogenase.- V. Phosphoenolpyruvic Carboxylase.- VI. Phosphoenolpyurvate Carboxykinase.- VII. Malic Enzyme.- C. The Glyoxalate Cycle.- I. Malate Synthetase.- II. Isocitritase.- D. Enzymes Related to the Glyoxalate Cycle.- I. Glycollic Acid Oxidase.- II. Glyoxalic Acid Reductase.- III. Glycolaldehyde Dehydrogenase.- IV. Glycine Oxidase.- V. Formic Dehydrogenase.- References.- Enzymes of Terminal Respiration.- A. Characterization of the Intact Respiratory Chain.- I. Measurement of Respiratory Rate.- 1. Manometry.- 2. Volumetry.- 3. Polarography.- 4. Spectrophotometry.- II. Effect of Oxygen Partial Pressure on Respiratory Rate.- 1. General Considerations.- 2. Methods.- III. Coupling to Phosphorylation.- 1. Manometric Method.- 2. Other Methods.- IV. The Use of Inhibitors.- 1. Oxidase Inhibitors.- 2. Inhibition within the Cytochrome System.- 3. Inhibition in the Flavoprotein Region.- V. Spectrophotometric Methods.- 1. Special Problems.- 2. Instruments.- 3. Procedures.- 4. Analysis of Results.- B. The Respiratory Chain Components.- I. DPNH Dehydrogenase.- 1. Diaphorase.- 2. Quinone Reductase.- 3. Cytochrome c Reductase.- 4. DPNH-Ferricyanide Reduction.- II. Transhydrogenase.- III. Cytochromes “b”.- IV. Cytochromes “c”.- V. Cytochrome Oxidase (a—a3).- VI. Lipid Components (Coenzyme Q).- C. Other Pathways to Oxygen.- I. From Pyridine Nucleotides to Oxygen.- 1. General Considerations.- 2. The Copper Oxidases.- a) Polyphenol Oxidase.- b) Laccase.- c) Ascorbic Acid Oxidase.- 3. Peroxidases.- 4. Glycolic Acid (?-Hydroxy Acid) Oxidase.- II. From other Substrates to Oxygen.- 1. Glucose Oxidase.- 2. Carbohydrate Oxidase.- References.- Summary of Recommendations on Enzyme Terminology. (By the Commission on Enzymes of the International Union of Biochemistry, 1961).- Enzyme units.- Symbols of enzyme kinetics.- The nomenclature of coenzymes.- Classification and nomenclature of cytochromes.- Classification and nomenclature of enzymes.- The terminology of enzyme formation.- “Appendix B”: Recommended Symbols for Enzyme Kinetics.- “Appendix C”: List of Cytochromes.- “Appendix D”: Key to Numbering and Classification of Enzymes.- Sachverzeichnis (Deutsch-Englisch).- Subject Index (English-German).- Table des Matières pour la Contribution: F. Chapeville et P. Fromageot, Enzymes du Métabolisme du Soufre.

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