Biomaterial Database

Changes in levels of alcohol dehydrogenase during the development of Drosophila melanogaster. 1981

S M Anderson, and J F McDonald

The results of an analysis of the biochemical basis of changes in alcohol dehydrogenase (E.C.1.1.1.1) activity over Drosophila development are presented. The data indicate that (1) the characteristic changes that occur in ADH activity over development are predominantly, it not exclusively, the result of quantitative changes in the amount of enzyme present rather than qualitative changes affecting the enzyme's specific activity and (2) the fluctuations in amount of ADH which occur during development are not the result of the only known form of post-translational modification capable of affecting the biochemical properties of the enzyme. We conclude that developmental changes in amount of ADH are most likely the result of fluctuations in the turnover of the ADH protein.

UI	MeSH Term	Description	Entries
D008675	Metamorphosis, Biological	Profound physical changes during maturation of living organisms from the immature forms to the adult forms, such as from TADPOLES to frogs; caterpillars to BUTTERFLIES.	Biological Metamorphosis,Biological Metamorphoses,Metamorphoses, Biological
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
D005786	Gene Expression Regulation	Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.	Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
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