-transparent.png){kind=logo}
Both aldehyde dehydrogenase (ALDH, EC 1.2.1.3) and the aldehyde dehydrogenase activity of alcohol dehydrogenase (ADH, EC 1.1.1.1) were found to coexist in Drosophila melanogaster larvae. The enzymes, however, showed different inhibition patterns with respect to pyrazole, cyanamide and disulphiram. ALDH-1 and ALDH-2 isoenzymes were detected in larvae by electrophoretic methods. Nonetheless, in tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme. The larval fat body probably was the major site of this pathway.
Related Publications
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
January 1991,
Genetica,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
April 1999,
Biochemical genetics,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
March 1988,
The Journal of nutrition,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
January 1994,
Alcohol and alcoholism (Oxford, Oxfordshire). Supplement,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
January 1985,
Experientia,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
February 1998,
The Biochemical journal,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
July 1995,
Proceedings of the National Science Council, Republic of China. Part B, Life sciences,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
August 2004,
Integrative and comparative biology,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
June 1988,
Heredity,
P W Heinstra, and
B W Geer, and
D Seykens, and
M Langevin
January 1985,
Molecular & general genetics : MGG,
