Article
Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase.
European journal of biochemistry - 5 Dec 1991
Chen Z, Lee W R, Chang S H
Abstract excerpt
Drosophila alcohol dehydrogenase (ADH), an NAD(+)-dependent dehydrogenase, shares little sequence similarity with horse liver ADH. However, these two enzymes do have substantial similarity in their secondary structure at the NAD(+)-binding domain [Benyajati, C., Place, A. P., Powers, D. A. & Sofer, W. (1981) Proc. Natl Acad. Sci. USA 78, 2717-2721]. Asp38, a conserved residue between Drosophila and horse liver...
Topics
- Alcohol Dehydrogenase
- Amino Acid Sequence
- Animals
- Aspartic Acid
- Binding Sites
- Blotting, Western
- Drosophila
- Electrophoresis, Polyacrylamide Gel
- Horses
- Hot Temperature
- Humans