Mechanisms of N-demethylation reactions catalyzed by cytochrome P-450 and peroxidases. 1985

P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis

UI MeSH Term Description Entries
D008862 Microsomes, Liver Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough. Liver Microsomes,Liver Microsome,Microsome, Liver
D010544 Peroxidases Ovoperoxidase
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450
D003640 Dealkylation The removing of alkyl groups from a compound. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Dealkylations
D003903 Deuterium The stable isotope of hydrogen. It has one neutron and one proton in the nucleus. Deuterons,Hydrogen-2,Hydrogen 2
D000588 Amines A group of compounds derived from ammonia by substituting organic radicals for the hydrogens. (From Grant & Hackh's Chemical Dictionary, 5th ed) Amine
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
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
May 1983, Molecular pharmacology,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
July 1999, Drug metabolism and disposition: the biological fate of chemicals,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
January 1991, Chemical research in toxicology,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
July 1986, Archives of biochemistry and biophysics,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
July 1989, Biochemical pharmacology,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
December 1983, Biochemical pharmacology,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
July 1980, The Journal of biological chemistry,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
April 1977, Archives of biochemistry and biophysics,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
January 1973, Drug metabolism and disposition: the biological fate of chemicals,
P F Hollenberg, and G T Miwa, and J S Walsh, and L A Dwyer, and D E Rickert, and G L Kedderis
January 1988, Annales de medecine interne,
Copied contents to your clipboard!