Drosophila melanogaster aldehyde dehydrogenase. 1985

M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens

Subcellular fractionation by differential centrifugation confirms the presence of aldehyde dehydrogenase in D. melanogaster. It is found principally in the heavy mitochondrial fraction.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008928 Mitochondria Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed) Mitochondrial Contraction,Mitochondrion,Contraction, Mitochondrial,Contractions, Mitochondrial,Mitochondrial Contractions
D002374 Catalase An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA. Catalase A,Catalase T,Manganese Catalase,Mn Catalase
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
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
D000444 Aldehyde Dehydrogenase An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70. D-Glucuronolactone Dehydrogenase,Aldehyde Dehydrogenase (NAD(+)),Aldehyde Dehydrogenase E1,Aldehyde Dehydrogenase E2,Aldehyde-NAD Oxidoreductase,Aldehyde NAD Oxidoreductase,D Glucuronolactone Dehydrogenase,Dehydrogenase, Aldehyde,Dehydrogenase, D-Glucuronolactone
D000445 Aldehyde Oxidoreductases Oxidoreductases that are specific for ALDEHYDES. Aldehyde Oxidoreductase,Oxidoreductase, Aldehyde,Oxidoreductases, Aldehyde
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
D013347 Subcellular Fractions Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163) Fraction, Subcellular,Fractions, Subcellular,Subcellular Fraction

Related Publications

M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
January 1991, Genetica,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
February 1998, The Biochemical journal,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
August 2004, Integrative and comparative biology,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
July 1993, Insect biochemistry and molecular biology,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
March 2008, Insect biochemistry and molecular biology,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
April 2006, Genetical research,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
January 1975, Methods in enzymology,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
January 1973, Journal of insect physiology,
M C Liétaert, and M Libion-Mannaert, and S Wattiaux-De Coninck, and A Elens
November 1970, Genetics,
Copied contents to your clipboard!