Kinetics of Alcohol Metabolizing Enzymes

Stone, Carol L.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute on Alcohol Abuse and Alcoholism (NIAAA)
• Type: Scientist Development Award (K21)
• Project #: 7K21AA000148-06
• Application #: 2042793
• Study Section: Biochemistry, Physiology and Medicine Subcommittee (ALCB)
• Project Start: 1996-09-01
• Project End: 1997-03-31
• Budget Start: 1996-09-01
• Budget End: 1997-03-31
• Support Year: 6
• Fiscal Year: 1996

Institution

• Name: Stevens Institute of Technology
• Department: Chemistry
• Type: Schools of Engineering
• City: Hoboken
• State: NJ
• Country: United States
• Zip Code: 07030

Publications

Davis, G J; Bosron, W F; Stone, C L et al. (1996) X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J Biol Chem 271:17057-61

Kedishvili, N Y; Bosron, W F; Stone, C L et al. (1995) Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes. J Biol Chem 270:3625-30

Stone, C L; Hurley, T D; Peggs, C F et al. (1995) Cimetidine inhibition of human gastric and liver alcohol dehydrogenase isoenzymes: identification of inhibitor complexes by kinetics and molecular modeling. Biochemistry 34:4008-14

Yang, Z N; Davis, G J; Hurley, T D et al. (1994) Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reduction. Alcohol Clin Exp Res 18:587-91

Stone, C L; Thomasson, H R; Bosron, W F et al. (1993) Purification and partial amino acid sequence of a high-activity human stomach alcohol dehydrogenase. Alcohol Clin Exp Res 17:911-8