PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1571363-7 1992 Kinetic studies revealed that the inhibition by chenodeoxycholic acid was competitive with respect to carnitine with an apparent Ki of 890 microM for carnitine acetyltransferase, 650 microM for carnitine octanoyltransferase and 600 microM for carnitine palmitoyltransferase. Carnitine 102-111 carnitine O-acetyltransferase Rattus norvegicus 150-177 9502050-6 1997 The observed changes in activity of CAT of heart might be due to theophylline-enhanced mobilization of lipid from adipose tissues which consequently stimulated increased L-carnitine transport into the heart tissues to form fatty acyl-carnitine groups for subsequent beta-oxidation inside the heart mitochondria. Carnitine 170-181 carnitine O-acetyltransferase Rattus norvegicus 36-39 9059510-8 1997 CAT activity positively correlated with the total and free carnitine levels in both liver and heart (r = 0.764, r = 0.785 and r = 0.700, r = 0.519, respectively). Carnitine 59-68 carnitine O-acetyltransferase Rattus norvegicus 0-3 7563233-5 1995 Carnitine acetyl transferase activity was stimulated by the treatment of l-carnitine in the hippocampus but it remained unchanged in the striatum and the cerebral cortex. Carnitine 73-84 carnitine O-acetyltransferase Rattus norvegicus 0-28 8207327-2 1994 Carnitine acetyltransferase occurs in several tissues and transfers acetyl groups from ACoA to carnitine forming acetylcarnitine and exhibits weak choline acetyltransferase activity. Carnitine 95-104 carnitine O-acetyltransferase Rattus norvegicus 0-27 8142416-2 1994 Carnitine acetyltransferase provides one of the control mechanisms for this ratio during changing energy demand in the heart muscle, possibly by buffering the CoA and carnitine concentration for sustained beta-oxidation. Carnitine 167-176 carnitine O-acetyltransferase Rattus norvegicus 0-27 3214166-17 1988 The combined data demonstrate further differences between the carnitine recognition sites in CPT and CAT. Carnitine 62-71 carnitine O-acetyltransferase Rattus norvegicus 101-104 2774175-1 1989 Carnitine acetyltransferase is used in a radioenzymatic assay to measure the concentration of carnitine. Carnitine 94-103 carnitine O-acetyltransferase Rattus norvegicus 0-27 1932127-11 1991 CAT activity appears to be critical for carnitine-mediated reversal of propionate-induced inhibition of pyruvate oxidation. Carnitine 40-49 carnitine O-acetyltransferase Rattus norvegicus 0-3 3624133-7 1987 Carnitine acetyltransferase (CAT) was significantly increased in heart by L-carnitine supplementation, whereas it was reduced by depletion in skeletal muscle. Carnitine 74-85 carnitine O-acetyltransferase Rattus norvegicus 0-27 3178716-1 1988 Relation between hepatic carnitine concentration and carnitine acetyltransferase activity. Carnitine 25-34 carnitine O-acetyltransferase Rattus norvegicus 53-80 3335535-4 1988 Carnitine greatly reduced the amounts of propionyl-CoA derived from alpha-ketoisovalerate, while smaller effects were obtained on the branched-chain acyl-CoA levels, consistent with the latter acyl moieties being poorer substrates for carnitine acetyltransferase and also poorer substrates for the carnitine/acylcarnitine translocase. Carnitine 0-9 carnitine O-acetyltransferase Rattus norvegicus 235-262 3624133-7 1987 Carnitine acetyltransferase (CAT) was significantly increased in heart by L-carnitine supplementation, whereas it was reduced by depletion in skeletal muscle. Carnitine 74-85 carnitine O-acetyltransferase Rattus norvegicus 29-32 15155769-2 2004 Carnitine acetyltransferases (CrAT) catalyze the reversible conversion of acetyl-CoA and carnitine to acetylcarnitine and free CoA. Carnitine 89-98 carnitine O-acetyltransferase Rattus norvegicus 0-28 3827937-18 1987 While MGBG appeared to be competitive with l-carnitine for both CPT and CAT, MGBG also exhibits a number of effects which may be mediated through membrane interaction and which are not reversed by carnitine. Carnitine 43-54 carnitine O-acetyltransferase Rattus norvegicus 72-75 3827937-18 1987 While MGBG appeared to be competitive with l-carnitine for both CPT and CAT, MGBG also exhibits a number of effects which may be mediated through membrane interaction and which are not reversed by carnitine. Carnitine 45-54 carnitine O-acetyltransferase Rattus norvegicus 72-75 3997872-9 1985 Free CoASH is also regenerated from S-acetyl-3-mercaptopropionyl-CoA and more rapidly from 3-mercaptopropionyl-CoA as a result of their reactions with carnitine catalyzed by carnitine acetyltransferase. Carnitine 151-160 carnitine O-acetyltransferase Rattus norvegicus 174-201 6722939-3 1984 Type 1 error occurs when endogenous substrates (e.g. L-carnitine) are acetylated by acetyltransferase enzymes (e.g. carnitine acetyltransferase ( CarAc ) ) yielding an acetylated product mistaken for acetylcholine (AcCh). Carnitine 53-64 carnitine O-acetyltransferase Rattus norvegicus 116-143 6722939-3 1984 Type 1 error occurs when endogenous substrates (e.g. L-carnitine) are acetylated by acetyltransferase enzymes (e.g. carnitine acetyltransferase ( CarAc ) ) yielding an acetylated product mistaken for acetylcholine (AcCh). Carnitine 53-64 carnitine O-acetyltransferase Rattus norvegicus 146-151 1220678-16 1975 Carnitine acetyltransferase (EC 2.3.1.7) activity measured in the same assay system in response to added l-carnitine was very low in normal rat liver homogenates, owing to the apparent high acetyl-CoA hydrolase activity, but was increased markedly after Sephadex treatment. Carnitine 105-116 carnitine O-acetyltransferase Rattus norvegicus 0-27 7359325-0 1980 Effect of carnitine analogs on carnitine acetyltransferase. Carnitine 10-19 carnitine O-acetyltransferase Rattus norvegicus 31-58 7359325-1 1980 Carnitine analogs with various substituents on the nitrogen were tested for their effect on carnitine acetyltransferase from rat sperm and pigeon breast. Carnitine 0-9 carnitine O-acetyltransferase Rattus norvegicus 92-119 16742571-22 1967 Comparison of the acetylation states of carnitine and CoA in perfused hearts suggests that the carnitine acetyltransferase reactants may remain near equilibrium despite wide variations in their steady-state concentrations. Carnitine 40-49 carnitine O-acetyltransferase Rattus norvegicus 95-122 15155769-2 2004 Carnitine acetyltransferases (CrAT) catalyze the reversible conversion of acetyl-CoA and carnitine to acetylcarnitine and free CoA. Carnitine 89-98 carnitine O-acetyltransferase Rattus norvegicus 30-34 11799139-10 2002 These results suggest that l-carnitine stimulates transcription of CPT1, CPT2, and CRAT as well as the enzyme activity of CPT1 in the livers of aged rats. Carnitine 27-38 carnitine O-acetyltransferase Rattus norvegicus 83-87 11799139-7 2002 Carnitine-fed old rats had a significant (p<0.05) 8-12-fold higher mean transcription rate of CPT1 and CRAT compared to aged controls, adult carnitine-fed animals, and adult controls, whereas the transcription rate of CPT2 was stimulated 2-3-fold in carnitine-fed animals of both age groups. Carnitine 0-9 carnitine O-acetyltransferase Rattus norvegicus 106-110