Enzymology and Molecular Biology of Carbonyl Metabolism 4

1. Retinoic Acid Synthesis in the Developing Retina

   • Peter McCaffery, Ursula C. Dräger

   Pages 181-190

2. Human Liver High Km Aldehyde Dehydrogenase (ALDH4): Properties and Structural Relationship to the Glutamic γ-Semialdehyde Dehydrogenase

   • Dharam P. Agarwal, Rolf Eckey, John Hempel, H. Werner Goedde

   Pages 191-197

3. Effect of Some Compounds Related to Disulfiram on Mitochondrial Aldehyde Dehydrogenase in Vitro and in Vivo

   • Trevor M. Kitson, Kathryn E. Kitson, Leong Goh

   Pages 199-209

4. Photoaffinity Labeling of Aldehyde Dehydrogenase from Horse Liver by P1-N6-(4-Azidophenylethyl)adenosine-P2-[4-(3-Azidopyridinio)Butyl] Diphosphate

   • Christoph Woenckhaus, Hanno Leibrock, Susanne Becker

   Pages 211-219

5. Aldehyde Dehydrogenase: Aldehyde Dehydrogenation and Ester Hydrolysis

   • Regina Pietruszko, Darryl P. Abriola, Erich E. Blatter, Neeta Mukerjee

   Pages 221-231

6. Is the Single Site Binding Model for Aldehyde Dehydrogenase an Oversimplification? The One-Site, Two-Site Debate Revisited

   • Jeremy P. Hill, Adrian F. Bennett, Paul D. Buckley, Rosemary L. Motion, Leonard F. Blackwell

   Pages 233-244

7. Crystallization and Preliminary X-ray Analysis of Bovine Mitochondrial Aldehyde Dehydrogenase and Human Glutathione-Dependent Formaldehyde Dehydrogenase

   • Thomas D. Hurley, Zhongning Yang, William F. Bosron, Henry Weiner

   Pages 245-250

8. The Aldo-Keto Reductases: an Overview

   • T. Geoffrey Flynn, Nancy C. Green

   Pages 251-257

9. Location of an Essential Arginine Residue in the Primary Structure of Pig Aldose Reductase

   • Terrance J. Kubiseski, Nancy C. Green, T. Geoffrey Flynn

   Pages 259-265

10. CYS298 is Responsible for Reversible Thiol-Induced Variation in Aldose Reductase Activity

    • Kurt M. Bohren, Kenneth H. Gabbay

    Pages 267-277

11. Substrate Specificity of Reduced and Oxidized Forms of Human Aldose Reductase

    • David L. Vander Jagt, Lucy A. Hunsaker

    Pages 279-288

12. Kinetic Alteration of Human Aldose Reductase by Mutagenesis of Cysteine Residues

    • J. Mark Petrash, Theresa Harter, Ivan Tarle, David Borhani

    Pages 289-300

13. 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

    • Walter H. J. Ward, Peter N. Cook, Donald J. Mirrlees, David R. Brittain, John Preston, Frank Carey et al.

    Pages 301-311

14. Sepiapterin Reductase and ALR2 (“Aldose Reductase”) from Bovine Brain

    • Thomas G. Dowling, John F. O’ Rourke, Keith. F. Tipton

    Pages 313-324

15. Polymorphisms of the Aldose Reductase Locus (ALR2) and Susceptibility to Diabetic Microvascular Complications

    • Ashok Patel, Suvina Ratanachaiyavong, B. Ann Millward, Andrew G. Demaine

    Pages 325-332

16. Polycyclic Aromatic Hydrocarbons and Phenolic Antioxidants do not Significantly Induce Carbonyl Reductase in Human Cell Lines

    • Barbara Ruepp, Bendicht Wermuth

    Pages 333-337

17. The Purification and Properties of a Novel Carbonyl Reducing Enzyme from Mouse Liver Microsomes

    • Edmund Maser

    Pages 339-350

18. Properties and Stereoselectivity of Carbonyl Reductases Involved in the Ketone Reduction of Warfarin and Analogues

    • J. J. R. Hermans, H. H. W. Thijssen

    Pages 351-360

19. Activation of Pulmonary Carbonyl Reductase by Aromatic Amines and Pyridine Ring-Containing Compounds

    • Akira Hara, Masaki Sakai, Toshihiro Nakayama, Yoshihiro Deyashiki, Hideo Sawada

    Pages 361-370

20. Unique Dihydrodiol Specific Dehydrogenase of Bovine Liver: Inhibition Studies and Comparison with Aldo/Keto Reductase

    • Hirofumi Nanjo, Tohru Nishinaka, Makoto Nagai, Tomoyuki Terada, Tadashi Mizoguchi, Tsutomu Nishihara

    Pages 371-377

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.

• biochemistry
• biology
• carbon
• chemistry
• enzyme
• enzymes
• enzymology
• metabolism
• molecular biology
• mutagenesis

• Purdue University, West Lafayette, USA

  Henry Weiner

• Indiana University School of Medicine and Veterans Administration Medical Center, Indianapolis, USA

  David W. Crabb

• Queens University, Kingston, Canada

  T. Geoffrey Flynn

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