Alcohol dehydrogenase of Drosophila melanogaster: metabolic differences mediated through cryptic allozymes. 1986

P W Heinstra, and W J Aben, and W Scharloo, and G E Thörig

Acetone formation from propan-2-ol, a saturated secondary alcohol, has been analysed in flies of three different Adh-genotypes of D. melanogaster. The in vivo oxidation of propan-2-ol was mainly mediated through ADH activity. It could be demonstrated that flies homozygous for the Adh71k allele produced more acetone than flies homozygous for AdhF. This difference in metabolic flux mediated through the cryptic allozymes under non-saturated ADH-substrate conditions seems to be based on their different kinetic properties in vivo. Product inhibition of ADH monitored by means of ADH-isozymes conversion as observed after electrophoresis was similar for both cryptic allozymes. ADH-71k and ADH-F showed immunological identity, and the in vivo protein levels of ADH-71k were 25-30 per cent higher than ADH-F. The population-genetic implications of our findings have been evaluated.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008297 Male Males
D004331 Drosophila melanogaster A species of fruit fly frequently used in genetics because of the large size of its chromosomes. D. melanogaster,Drosophila melanogasters,melanogaster, Drosophila
D006720 Homozygote An individual in which both alleles at a given locus are identical. Homozygotes
D000426 Alcohol Dehydrogenase A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. Alcohol Dehydrogenase (NAD+),Alcohol Dehydrogenase I,Alcohol Dehydrogenase II,Alcohol-NAD+ Oxidoreductase,Yeast Alcohol Dehydrogenase,Alcohol Dehydrogenase, Yeast,Alcohol NAD+ Oxidoreductase,Dehydrogenase, Alcohol,Dehydrogenase, Yeast Alcohol,Oxidoreductase, Alcohol-NAD+
D000429 Alcohol Oxidoreductases A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99). Carbonyl Reductase,Ketone Reductase,Carbonyl Reductases,Ketone Reductases,Oxidoreductases, Alcohol,Reductase, Carbonyl,Reductase, Ketone,Reductases, Carbonyl,Reductases, Ketone
D000433 1-Propanol A colorless liquid made by oxidation of aliphatic hydrocarbons that is used as a solvent and chemical intermediate. Alcohol, Propyl,Propanol,n-Propanol,Propyl Alcohol
D000483 Alleles Variant forms of the same gene, occupying the same locus on homologous CHROMOSOMES, and governing the variants in production of the same gene product. Allelomorphs,Allele,Allelomorph
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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