Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Low dietary protein has been shown to induce the activity of rat hepatic UDP-glucuronyltransferase (UDPGTase) as measured in vitro. The assay of UDPGTase in vitro is hampered by the need to solubilize the microsomal membrane, without destroying the physiological significance of the measurements. The present work was to determine the effect of dietary protein on the activity of UDPGTase and on the activity of UDP-glucose dehydrogenase. Chloral hydrate induced sleeping time was used as a bioassay for UDPGTase, confirming the physiological significance of the in vitro analysis. Sixty male rats were maintained on three different protein levels (7.5, 15, and 45%) for 16 days. Fifteen rats from each group were sacrificed and hepatic UDPGTase, cytochrome P-450, UDP-glucose dehydrogenase, and alcohol dehydrogenase were assayed. Five rats from each group were dosed with 7.5% chloral hydrate (4.8 mL/kg body weight) to measure sleeping time. Rats on 7.5% dietary protein had significantly higher UDPGTase activity than rats fed either 15 or 45% protein diets. These differences in enzyme activity in vitro correlated with the differences in chloral hydrate sleeping time. Dietary protein was not found to affect the activity of UDP-glucose dehydrogenase as measured in vitro.
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PMID:The effect of dietary protein quantity on the activity of UDP-glucuronyltransferase and its physiological significance in drug metabolism. 681 86

To clarify species differences in the metabolism of di(2-ethylhexyl) phthalate (DEHP) we measured the activity of four DEHP-metabolizing enzymes (lipase, UDP-glucuronyltransferase (UGT), alcohol dehydrogenase (ADH), and aldehyde dehydrogenase (ALDH)) in several organs (the liver, lungs, kidneys, and small intestine) of mice (CD-1), rats (Sprague-Dawley), and marmosets (Callithrix jacchus). Lipase activity, measured by the rate of formation of mono(2-ethylhexyl) phthalate (MEHP) from DEHP, differed by 27- to 357-fold among species; the activity was highest in the small intestines of mice and lowest in the lungs of marmosets. This might be because of the significant differences between Vmax/Km values of lipase for DEHP among the species. UGT activity for MEHP in the liver microsomes was highest in mice, followed by rats and marmosets. These differences, however, were only marginal compared with those for lipase activity. ADH and ALDH activity also differed among species; the activity of the former in the livers of marmosets was 1.6-3.9 times greater than in those of rats or mice; the activity of the latter was higher in rats and marmosets (2-14 times) than in mice. These results were quite different from those for lipase or UGT activity. Because MEHP is considered to be the more potent ligand to peroxisome proliferator-activated receptor alpha involved in different toxic processes, a possibly major difference in MEHP-formation capacity could be also considered on extrapolation from rodents to humans.
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PMID:Species differences in the metabolism of di(2-ethylhexyl) phthalate (DEHP) in several organs of mice, rats, and marmosets. 1579 88