Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Kynurenine transaminase activity in rat kidney was found in both the mitochondrial and supernatant fractions. These fractions contained (a) kynurenine pyruvate transaminase, which showed a preference for pyruvate as amino acceptor, and had a pH optimum between 8.0 and 8.5, and (b) kynurenine 2-oxoglutarate transaminase, with a preference for 2-oxoglutarate and a pH optimum between 6.0 and 6.5. The apparent Km value of the former enzyme for L-kynurenine was much lower than that of the latter enzyme.
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PMID:Subcellular distribution and properties of kynurenine pyruvate transaminase in rat kidney. 24 Jul 68

The activities of tryptophan 2,3-dioxygenase (EC 1.13.11.11), indoleamine 2,3-dioxygenase (EC 1.13.11.17), kynurenine 3-hydroxylase (EC 1.14.13.9), kynureninase (EC 3.7.1.3), kynurenine transaminases, and pyridoxal phosphokinase (EC 2.7.1.35) in the liver, kidney and lung rats were measured after administration of a single dose and repeated doses of dimethoate, carbaryl and fenvalerate, respectively. Ten percent LD50 of each insecticide was orally administered to a rat for a single dose, while 5% LD50 was orally given for five consecutive days as repeated doses. The control animals received the same volume of vehicle (polyethylene glycol 300). Body weight and organs weight losses were recognized only after repeated doses of dimethoate, while protein content remained constant compared to control animals. Repeated administration of dimethoate caused significant decrease in the activity of kynurenine 3-hydroxylase (28.3% decrease in liver, and 32.5% in kidney), kynurenine-pyruvate transaminase (EC 2.6.1.7) (40% in liver, and 24.2% in kidney), kynurenine- pyruvate transaminase (EC 2.6.1-) (24.5% in kidney) and pyridoxal phosphokinase (36.1% in liver). Repeated doses of carbaryl resulted in a significant decrease in the activity of apo-tryptophan 2,3-dioxygenase (42.8%), kynurenine-2-oxoglutarate transaminase (40% in liver), kynurenine-pyruvate transaminase (30.6% in liver), and serine-glyoxylate transaminase (EC 2.6.1.51) (47.9% in liver). Externally added insecticides at different concentrations to the incubation mixture resulted in an inhibition to tryptophan 2,3-dioxygenase, while the other enzymes examined showed no change in their activities.
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PMID:Effects of some insecticides on several enzymes of tryptophan metabolism in rats. 211 99