Enzymology and Molecular Biology of Carbonyl Metabolism 6

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 Once again, the willingness of the participants to discuss unpublished data and to share thoughts about the future directions of their research helped make this, like our previous seven meetings, a special scientific experience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.

Zusammenfassung
Proceedings of the 8th International Workshop held in Deadwood, South Dakota, June 29-July 3, 1996

Inhalt
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. Jörnvall, 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. Höög, 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.