Carnitine

(redirected from carnitine acetyltransferase)
Also found in: Dictionary, Medical, Acronyms.
Related to carnitine acetyltransferase: carnitine palmitoyltransferase

carnitine

[′kär·nə‚tēn]
(biochemistry)
C7H15NO3α-Amino-β-hydroxybutyric acid trimethylbetaine; a constituent of striated muscle and liver, identical with vitamin B T.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

Carnitine

 

betaine-γ-amino-β-oxybutyric acid, (CH3)3NCH2CH(OH)CH2CO2, a crystalline compound with basic properties; dissolves readily in water and alcohol. Its molecular mass is 161.21, and its melting point, 195°-197°C (with decomposition).

Carnitine is primarily found in animal muscle, from which it was first extracted by V. S. Gulevich (1905); it is also found in bacteria and plants. It takes part in fatty exchange within an organism by acting as a carrier of fatty acid radicals through the membranes of the mitochondria. These membranes are impermeable to activated fatty acids (compounds with coenzyme A). With the aid of carnitine, therefore, fatty acids enter the scope of activity of the oxidizing enzymes localized within the mitochondria. Carnitine apparently also participates in the reverse transport of fatty acids. It is an essential dietary constituent and a growth factor in certain insects; therefore it is considered to be a vitamin (vitamin BT).

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
One may therefore postulate that increased activities of fatty acid synthetase, ketoglutarate, glucose-o-phosphate dehydrogenase, and carnitine acetyltransferase may be part of an adaptive response of megakaryocytes to the increased influx of glucose through the GLUT 3 glucose transporter (Table 2) (9).
As shown in Table 2, diabetes caused increases in the activities of glucose-o-phosphate dehydrogenase (17%) carnitine acetyltransferase (21%), 2-oxoglutarate dehydrogenase (37%), and fatty acid synthetase (62%), but we found no significant changes in citrate synthase activity (Table 2).
The activities of fatty acid synthetase, ketoglutarate dehydrogenase (EC 1.2.4.2), carnitine acetyltransferase, glucose-6-phosphate dehydrogenase (EC 1.1.1.49), and citrate synthase were assayed by methods described elsewhere (17-21).