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like at all our previous meetings, the extreme openness of the participants to discuss ideas, future directions and unpublished data.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.

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 theInduction 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 DeterminingSubstrate 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 Properties.- 43. Mammalian Class VI Alcohol Dehydrogenase: Novel Types of the Rodent Enzymes.- 44. Crystallizations of Novel Forms of Alcohol Dehydrogenase.- 45. Human Sorbitol Dehydrogenase Gene: cDNA Sequence and Expression.- 46. Short-Chain Dehydrogenases/Reductases.- 47. Zinc Binding of Alcohol and Sorbitol Dehydrogenases.- 48. Horse Liver Alcohol Dehydrogenase-Catalyzed Aldehyde Oxidation: The Sequential Oxidation of Alcohols to Carboxylic Acids under NADH Recycling Conditions.- 49. Analytical Approaches to Alcohol Dehydrogenase Structures.- 50. Purification and Characterization of S-Formylglutathione Hydrolase from Human, Rat and Fish Tissues.- 51. Useful Mutants of Zymomonas Mobilis Alcohol Dehydrogenase-2 Obtained by the Use of Polymerase Chain Reaction Random Mutagenesis.