Enzymology and Molecular Biology of Carbonyl Metabolism No. 12 (illustrated Edition)

Enzymology and Molecular Biology of Carbonyl Metabolism No. 12 (illustrated Edition)

By: Henry Weiner (editor)Paperback

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This is the 12th volume in the Enzymology and Molecular Biology of Carbonyl Metabolism series. Within the text, the reader is given further valuable insight into Carbonyl Metabolism. This collection is the largest in its field of study and provides the deepest look into just three gene families. Through dozens of articles, molecular biological techniques are discussed, examining ways in which they are influencing the direction of research on Aldehyden Dehydrogenase, Alcohol Dehydrogenase, and Reductases.


Aldehyde Dehyrogenase; 1. An Update Of The Aldh Gene Superfamily. 2. Residue Conservations in Aldehyde Dehydrogenase Gene Fusion Products Reemphasize Functional Interpretations. 3. Role of Human Aldehyde Dehydrogenases in Ethylene Glycol Ether Metabolism: Oxidation of 2-Butoxyethanal and 2-Phenoxyethanal. 4. Screening for Variants of Human Liver Cytosolic Aldehyde Dehydrogenase with Altered Properties. 5. Acetaldehyde Elimination Changes in Transgenic Mice Lacking Aldehyde Dehydrogenase 2 Activity. 6. Accumulation of Hepatic Acetaldehyde and Reduced Alcohol Drinking in Transgenic Mice Carrying the Oriental Variant of the Human Aldehyde Dehydrogenase 2 Gene. 7. Aldh3al Is A Multifunctional Protein That Protects Against Oxidative Damage. 8. Aldehyde Dehydrogenase Gene Knockouts Provide Insight into Role of Retinoic Acid during Eye Development. 9. Role Of Retinal Dehydrogenase Type 1 (RALDH1, ALDH1A1) In Retinoic Acid Biosynthesis. 10. 4-Hydroxy-Trans-2-Nonenal Is Oxidized By ALDH3A And ALDH5A In The Human Brain. 11. Detoxification of Chloroacetaldehyde by Aldehyde Dehydrogenases Present in Human Kidney. 12. Inhibition of Cytosolic Aldehyde Dehydrogenase by Arachidonic Acid in Human Lung Tumor Cells A549. 13. Lack of Inducibility of Antiquitin (ALDH7A1) in Cultured Human Embryonic Kidney (HEK293) Cell Under Osmotic or Oxidative Stress. 14. Effects of Monovalent and Divalent Cations on the Thermostability of Porcine Kidney Betaine Aldehyde Dehydrogenase. 15. Functional and Structural Properties of Betaine Aldehyde Dehydrogenase, a Key Enzyme and Potential Drug Target in Pseudomonas aeruginosa. 16. Several Cytochromes P450 Are Aldehyde Monooxygenases; 17. Methylmalonate Semialdehyde Dehydrogenase From Bacillus Subtilis. Alcohol Dehydrogenase; 1. MDR Alcohol Dehydrogenases - Novel Forms and Possibilities. 2. Evolution of Cinnamyl Alcohol Dehydrogenase Family. 3. Mammalian Alcohol Dehydrogenase 3 (ADH3) Has Several Essential Functions. 4. Pharmacogenetic Determinants of Alcohol Metabolism and Alcoholism in the Human Alcohol Dehydrogenase Family. 5. Role of Carbonyl Metabolizing Enzymes in the Hepatocyte Cytotoxicity of Chloral Hydrate and Tribromoethanol anesthetics. 6. Structural Plasticity in Alcohol Dehydrogenase: How an NADP(H)-Dependent Enzyme Becomes Specific for NAD(H). 7. Human Alcohol Dehydrogenase 4: Mechanism, Specificity and Effects of Ethanol on Retinoid Metabolism. 8. Activity of Alcohol Dehydrogenase With 11-Cis-Retinoids And Distribution of ADH4 in Ocular Tissues. 9. Role of Carbonyl Metabolising Enzymes in the Anesthesia and Hepatotoxicity Induced by Chloral Hydrate and Tribromoethanol in vivo and in vitro. 10. The Structure of Benzyl Alcohol Dehydrogenase from Acinetobacter Calcoaceticus. 11. Reductases; 1. SDR Goes SGC- A Structural Genomics Initiative. 2. A Cosubstrate Specificity Determinant in Aldo-Keto Reductases. 3. Contribution of Aldo-Keto Reductases to the Metabolism of the Novel Anticancer Drug Oracin in Man. 4. Metabolism of Phospholipid Aldehydes: Role of Aldose Reductase. 5. Hepatocyte Methylglyoxal (MG) Resistance is Overcome by Inhibiting Aldo-Keto Reductases (Akrs) and Glyoxalase I (GLO I) Catalyzed MG Metabolism. 6. Search for Effective Aldose Reductase Inhibitors. 7. Regulation Of NF-aB By Aldose Reductase Is Hyperglycemia. 8. Enzymatic Mechanism Of 5a-Dihydrotestosterone Reduction Catalyzed By Human Type 3 3a-Hydroxysteroid Dehydrogenase (AKR1C2): Molecular Docking And Kinetic Studies. Comparison of the Rate-Limiting Steps in 3a-Hydroxysteroid Dehydrogenase (AKR1C9) Catalyzed Reactions. 9. Structural Aspects of Oligomerization in 3a-Hydroxysteroid Dehydrogenase/Carbonyl Reductase from Comamonas Testosteront: New Approaches for Efficient Protein Design. 10. Characterization Of Repressors Repa And Repb of the Steroid-Inducible 3a-Hydroxysteroid Dehydrogenase/Carbonyl Reductase In Comamonas Testosteront by Gene Knock Out Studies. 11. Site-Directed Mutagenesis of Residues in Coenzyme-Binding Sites of Mouse 3[alpha]- and 3(17)[alpha]-Hydroxysteroid Dehydrogenases: Their Roles in the Specificity for Coenzymes and Substrates. 12. Stereo-Specificity of 3- and 20-Ketosteroid Reduction Catalyzed by Human Aldo-Keto-Reductases AKR1C1-AKR1C4: Different Outcomes with 5[alpha]-Dihydrotestosterone (5[alpha]-DHT), Tibolone (A Synthetic 19-Norsteroid) And Progesterone. 13. Comparison Of Stereoselective Reduction of 3- and 20-Oxosteroids among Mouse and Primate 20[alpha]-Hydroxysteroid Dehydrogenases. 14. Further Insight into the Structural Basis of Coenzyme and Substrate Specificity of Fungal 17b-Hydroxysteroid Dehydrogenase. 15. Purification, Crystallization, X-Ray Diffraction Analysis and Phasing of a Fungal 17a-Hydroxysteroid Dehydrogenase. 16. Dysregulation of Human AKR1C Family Members in Human Breast Cancer. 17. Metabolism of the Lipid Peroxidation Product - 4-Hydroxy-Trans-2-Nonenal (HNE) in the Ischemic Heart. 18. Succinic Semialdehyde Reductases: Contribution to [alpha]-Hydroxybutyrate Catabolism and Subcellular Localization. 19. 1-Pyrroline-5'-Carboxylate Reductase is an Evolutionarily Distant Member of the [beta]-Hydroxyacid Dehydrogenase Enzyme Family. 20. Structure-Function Relationships for Candida Tenuis Xylose Reductase (AKR2B5): Properties of H113E Mutant. 21. Mutation of Lys-274 into Glutamate Disrupts the Coenzyme Binding Site of Xylose Reductase from Candida Tenuis (AKR2B5). 22. Functional Plasticity of Medium-Chain Dehydrogenases/Reductases.

Product Details

  • ISBN13: 9781557533845
  • Format: Paperback
  • Number Of Pages: 550
  • ID: 9781557533845
  • ISBN10: 1557533849
  • edition: illustrated Edition

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