1. Site Directed Mutagenesis to Probe for Active Site Components of Liver Mitochondrial Aldehyde Dehydrogenase.- 2. Substrate Binding Pocket Structure of Human Aldehyde Dehydrogenases: A Substrate Specificity Approach.- 3. Human Class 1 Aldehyde Dehydrogenase: Expression and Site-Directed Mutagenesis.- 4. Nitrate Esters as Inhibitors and Substrates of Aldehyde Dehydrogenase.- 5. Use of a Chromophoric Reporter Group to Probe the Active Site of Cytosolic Aldehyde Dehydrogenase.- 6. Studies of the Esterase Activity of Cytosolic Aldehyde Dehydrogenase Using Sterically Hindered and Cyclic Substrates.- 7. The Reduction of Propionic Anhydride by Aldehyde Dehydrogenase-Nadh Mixtures at pH 7.- 8. Cloning and Characterisation of the cDNA for Sheep Liver Cytosolic Aldehyde Dehydrogenase.- 9. Crystallization of Sheep Liver Cytosolic Aldehyde Dehydrogenase in a Form Suitable for High Resolution X-Ray Structural Analysis.- 10. Progress toward the Tertiary Structure of (Class 3) Aldehyde Dehydrogenase.- 11. UDP-Glucose Dehydrogenase: Structural Characteristics.- 12. Kinetic Studies on Class 3 Aldehyde Dehydrogenase from Bovine Cornea.- 13. Covalent Modification of Class 2 and Class 3 Aldehyde Dehydrogenase by 4-Hydroxynonenal.- 14. Constitutive and Overexpressed Human Cytosolic Class-3 Aldehyde Dehydrogenases in Normal and Neoplastic Cells/Secretions.- 15. Metabolism of Cyclophosphamide by Aldehyde Dehydrogenases.- 16. Tissue-Specific Expression and Preliminary Functional Analysis of the 5? Flanking Regions of the Human Mitochondrial Aldehyde Dehydrogenase (ALDH2) Gene.- 17. Transgenesis of the Aldehyde Dehydrogenase-2 (ALDH2) Locus in a Mouse Model and in Cultured Human Cells.- 18. Class 3 Aldehyde Dehydrogenase: A Northern Perspective in the Land Down Under.- 19. Studies on the Induction of Rat Class 3 Aldehyde Dehydrogenase.- 20. Mouse Class 3 Aldehyde Dehydrogenases.- 21. Cloning and Characterization of Genes Encoding Four Additional Human Aldehyde Dehydrogenase Isozymes.- 22. New Human Aldehyde Dehydrogenases.- 23. Retinoic Acid Synthesizing Enzymes in the Embryonic and Adult Vertebrate.- 24. Retinoic Acid Synthesis in the Developing Spinal Cord.- 25. Structure and Mechanism of Aldehyde Reductase.- 26. Expression of Human and Rat Carbonyl Reductase in E. coli: Comparison of the Recombinant Enzymes.- 27. Molecular Cloning and Sequencing of Mouse Hepatic 11ss-Hydroxysteroid Dehydrogenase/Carbonyl Reductase: A Member of the Short Chain Dehydrogenase Superfamily.- 28. Molecular Modelling Calculations on the Binding of D- and L-Xylose to Wild-Type Aldose Reductase and Its H11OQ and H11OA Mutants.- 29. Stopped-Flow Studies of Human Aldose Reductase Reveal which Enzyme Form Predominates during Steady-State Turnover in Either Reaction direction.- 30. Lysine Residues in the Coenzyme-Binding Region of Mouse Lung Carbonyl Reductase.- 31. Substrate Specificity and Kinetic Mechanism of Tetrahymena 20?-Hydroxysteroid Dehydrogenase.- 32. Purification and Characterization of Recombinant Human Placental and Rat Lens Aldose Reductases Expressed in Escherichia coli.- 33. Rat and Human Bile Acid Binders Are Members of the Monomeric Reductase Gene Family.- 34. The Alcohol Dehydrogenase System.- 35. Promoters of the Mammalian Class III Alcohol Dehydrogenase Genes.- 36. Class I and Class Iv Alcohol Dehydrogenase (Retinol Dehydrogenase) Gene Expression in Mouse Embryos.- 37. Molecular Evolution of Class I Alcohol Dehydrogenases in Primates: Models for Gene Evolution and Comparison of 3? Untranslated Regions of cDNAS.- 38. the Role of Leucine 116 in Determining Substrate Specificity in Human B1 Alcohol Dehydrogenase.- 39. Mutations of Human Class III Alcohol Dehydrogenase.- 40. Human and Rat Class IV Alcohol Dehydrogenases: Correlations of Primary Structures with Enzymatic Properties.- 41. Cloning and Expression of a Human Stomach Alcohol Dehydrogenase Isozyme.- 42. Purification and Properties of Murine Corneal Alcohol Dehydrogenase: Evidence for Class IV ADH P

Aldehyde Dehydrogenases-The 1992 Perspective.- Metabolic Role of Aldehyde Dehydrogenase.- Effects of Aldehyde Products of Lipid Peroxidation on the Activity of Aldehyde Metabolizing Enzymes in Hepatomas.- Metabolic Interactions of 4-Hydroxynonenal, Acetaldehyde and Glutathione in Isolated Liver Mitochondria.- Biological Role of Human Cytosolic Aldehyde Dehydrogenase 1: Hormonal Response, Retinal Oxidation and Implication in Testicular Feminization.- Human Cytosolic Aldehyde Dehydrogenase in Androgen Insensitivity Syndrome.- The Use of Immortalized Mouse L1210/OAP Cells Established in Culture to Study the Major Class 1 Aldehyde Dehydrogenase-Catalyzed Oxidation of Aldehydes in Intact Cells.- Enhanced Transcription of the Cytosolic ALDH Gene in Cyclophosphamide Resistant Human Carcinoma Cells.- Attempts to Increase the Expression of Rat Liver Mitochondrial Aldehyde Dehydrogenase in E. coli by Altering the mRNA.- Preliminary Characterization of the Rat Class 3 Aldehyde Dehydrogenase Gene.- Human High-Km Aldehyde Dehydrogenase (ALDH3): Molecular, Kinetic, and Structural Features.- Overexpression or Polycyclic Aromatic Hydrocarbon-Mediated Induction of an Apparently Novel Class 3 Aldehyde Dehydrogenase in Human Breast Adenocarcinoma Cells and Its Relationship to Oxazaphosphorine-Specific Acquired Resistance.- Tumor-Associated Aldehyde Dehydrogenase (ALDH3): Expression in Different Human Tumor Cell Lines with and without Treatment with 3-Methylcholanthrene.- Sexual Differentiation in the Induction of the Class 3 Aldehyde Dehydrogenase.- Mouse Class 3 Aldehyde Dehydrogenases: Positive and Negative Regulation of Gene Expression.- Human Stomach Aldehyde Dehydrogenase, ALDH3.- Bovine Corneal Aldehyde Dehydrogenases: Evidence for Multiple Gene Products (ALDH3 and ALDHX).- Carbonyl-Metabolizing Enzymes and Their Relatives Recruited as Structural Proteins in the Eye Lens.- Members of the ALDH Gene Family are Lens and Corneal Crystalline.- Retinoic Acid Synthesis in the Developing Retina.- Human Liver High Km Aldehyde Dehydrogenase (ALDH4): Properties and Structural Relationship to the Yeast Glutamic ?-Semialdhyde Dehydrogenase.- Effect of Some Compounds Related to Disulfiram on Mitochondrial Aldehyde Dehydrogenase in Vitro and in Vivo.- Photoaffinity Labeling of Aldehyde Dehydrogenase from Horse Liver by P1-N6-(4-Azidophenylethyl) Adenosine-P2[4-(3-Azidopyridinio)Butyl] Diphosphate.- Aldehyde Dehydrogenase: Aldehyde Dehydrogenation and Ester Hydrolysis.- Is the Single Site Binding Model for Aldehyde Dehydrogenase an Oversimplification? The One-Site, Two-Site Debate Revisited.- Crystallization and Preliminary X-Ray Analysis of Bovine Mitochondrial Aldehyde Dehydrogenase and Human Glutathione-Dependent Formaldehyde Dehydrogenase.- Aldo-Keto Reductases: An Overview.- Location of an Essential Arginne Residue in the Primary Structure of Pig Aldose Reductase.- Cys298 Is Responsible for Reversible Thiol-Induced Variation in Aldose Reductase Activity.- Substrate Specificity of Reduced and Oxidized Forms of Human Aldose Reductase.- Kinetic Alteration of Human Aldose Reductase by Mutagenesis of Cysteine Residues.- Inhibition of Aldose Reductase by (2, 6-Dimethylphenylsulphonyl) Nitromethane: Possible Implications for the Nature of an Inhibitor Binding Site and a Cause of Biphasic Kinetics.- Sepiapterin Reductase and ALR2 ("Aldose Reductase") from Bovine Brain.- Polymorphisms of the Aldose Reductase Locus (ALR2) and Suseptibility to Diabetic Microvascular Complications.- Polycyclic Aromatic Hydrocarbons and Phenolic Antioxidants do not Significantly Induce Carbonyl Reductase in Human Cell Lines.- The Purification and Properties of a Novel Carbonyl Reducing Enzyme from Mouse Liver Microsomes.- Properties and Stereoselectivity of Carbonyl Reductases Involved in the Ketone Reduction of Warfarin and Analogues.- Activation of Pulmonary Carbonyl Reductase by Aromatic Amines and Pyridine Ring-Containing Compounds.- Unique Dihydrodiol Specific Dehydrogena...

This volume contains information on aldehyde dehydrogenase, alcohol dehydrogenase, short- and medium-chain dehydrogenase, and reductases. Sixty-nine contributions provide a wide variety of information on enzymology, molecular biology, and metabolic aspects of these carbonyl metabolizing oxido-reductases. Much new information is provided, including previously unreported three-dimensional structures of enzymes and new aspects of gene regulation, along with sequence alignments, metabolism and enzyme mechanisms.

Aldehyde Dehydrogenase. Crystal Structure of a Class 3 Aldehyde Dehydrogenase at 2.6angstrom Resolution; Z-J. Liu, et al. Conserved Residues in the Aldehyde Dehydrogenase Family: Locations in the Class 3 Tertiary Structure; J. Hempel, et al. Class 3 Aldehyde Dehydrognease: A View from the Hills; R. Lindahl, et al. Human Corneal and Lens Aldehyde Dehydrogenases: Purification and Properties of Human Lens ALDH1 and Differential Expression as Major Soluble Proteins in Human Lens (ALDH1) and Cornea (ALDH3); G. King, R. Holmes. Alcohol Dehydrogenase. Alcohol Dehydrogenase Variability: Evolutionary and Functional Conclusions from Characterization of Further Variants; H. Joernvall, et al. Three-Dimensional Structures of Human Alcohol Dehydrogenase Isoenzymes Reveal the Molecular basis for Their Functional Diversity; T.D. Hurley, et al. Mammalian Class II Alcohol Dehydrogenase: A Highly Variable Enzyme; J.-O. Hoeoeg, S. Svensson. Activity of Liver Alcohol Dehydrogenases on Steroids; D.K. Wilson, et al. Aldo/Keto Reductases. Structural Studies of Aldo-Keto Reductase Inhibition; D.K. Wilson, et al. Aldehyde Reductase: Catalytic Mechanism and Substrate Recognition; O.A. Barski, et al. Study of Non-Covalent Enzyme-Inhibitor Complexes of Aldose Reductase by Electrospray Mass Spectrometry; N. Potier, et al. 55 Additional Articles. Index.

Since 1982, our ever-expanding group of investigators has been meeting in exotic parts of the world to discuss aspects of three enzyme systems. The 1996 meeting was no exception. Nearly 90 scientists from 15 countries met in the small city of Deadwood, South Dakota, for four days of stimulating talks and posters and incredible scenery. Once more this meeting reflected the changing trends in biochemical research. At the 1982 meeting most of the speakers discussed isolating new enzymes and trying to characterize them. At this meeting many speakers discussed interpretations of three-dimensional struc ture or regulatory elements of the genes controlling for the tissue-specific expression of the enzyme. Hopefully, readers will find the proceedings of the meeting to be of interest. Though they reflects the scientific information that was presented at the meeting, they do not indicate the level of personal interactions that went on during the meeting. Once again, the willingness of the participants to discuss unpublished data and to share thoughts about the future directions of their research helped make this, like our previous seven meetings, a special scientific experience for those who attended.

Since the inception of these meetings in 1982, they have always been a satellite of the International Society for Biomedical Research on Alcoholism meeting. At our 1992 meeting in Dublin we learned that the next ISBRA meeting would be held in Brisbane, of all our previous meetings, I was very concerned Australia. As the scientific organizer about holding a meeting in the Southern Hemisphere for fear that many of our potential participants would not travel that far. I am pleased to say that I was proven to be incorrect. Nearly 90 scientists from a dozen countries participated at our seventh conference. At this meeting, like at all our previous ones, much new information about the three enzyme systems was presented. Of equal importance was, like at all our previous meetings, the extreme openness of the participants to discuss ideas, future directions and unpublished data. On behalf of all the participants I wish to express our sincere thanks to our Massey University colleagues for the excellent organization of this Palmerston North, New Zealand meeting. These included Kathryn Kitson, Michael Hardman, Paul Buckley, Trevor Kitson and Len Blackwell. At this meeting a few new innovations were introduced. Though posters are common at many meetings, bush walks and visits to nature preserves to see kiwi birds Our hosts were able to secure support from the International Union of Biochemistry are not.

The Sixth International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism was held outside of Dublin, Ireland at the end of June, 1992. Prof. Keith Tipton, Chairman of the Biochemistry Department at Trinity College, kindly agreed to host the meeting. On behalf of all of us who attended I wish to extend our sincere thanks to the whole Tipton family for making us feel so welcome in Ireland. It has been a decade since the frrst workshop was held in Bern, Switzerland. The scope of the meetings reflected somewhat the changes that have occurred in biochemistry during the past decade. At the first meeting primarily enzymes and their properties were discussed. At this last meeting many of the talks centered on gene regulation as well as more traditional aspects of enzymology and metabolism. During the past decade site directed mutagenesis to probe for the active site of an enzyme has become part of traditional enzymology; this was virtually unheard of at our frrst meeting. Many of the presenters now used this tool to study some aspect of structure and function of one of the three carbonyl metabolizing enzymes.

Prior to the start of the eighth meeting, I had the good sense to ask Professor Rosa Angela Canuto of Turin, Italy if she would help me organize the ninth meeting. She quickly suggested that both she and Dr. Guiliana Muzio, also of Turin, help plan the meet ing. Each of our previous eight meetings was a unique experience for the participants. The science was always outstanding and the presentations and discussions were excellent. By moving each meeting to a different part of the world we were able to experience exciting foods and cultural aspects of the world in addition to the science. The ninth meeting was no exception. We met from June 18 to 22 in the small mountain city of Varallo, Italy, the birth place of Dr. Canuto. Holding the scientific sessions in a several-hundred-year-old converted mansion and having an afternoon trip to either Lago Maggiore or Monte Rosa made some aspects of this meeting extremely memorable. An additional unique aspect of the social portion of the meeting was our ability to invite the townspeople to share with us a concert performed in an old church. Though the social and cultural aspects of the meeting were outstanding, the pur pose of the meeting was to exchange scientific information about the status of the three enzyme systems.

The Fifth International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism was held at Purdue University in June, 1990. This represents the fifth time that I had the privilege of organizing the scientific program. It was the first time that I actually hosted the meeting. I wish to salute my four previous co-organizers and the thousands of scientists who have hosted other meetings. It is much easier to arrange the scientific program and edit the proceedings. No local organization could occur without the help of ones research group and, in this case, my wife. I sincerely thank Esther and my research group for their advise and help. At this Workshop, similar to the preceeding ones, much new information was presented. It was apparent how molecular biological techniques were influencing the direction of the research on the three families of enzymes discussed. It also was apparent that not all biochemical problems could be solved by using these techniques. Many of the presentations showed how important advances still could be made using more traditional biochemical approaches.