4-Bromo-2-octenoic acid specifically inactivates 3-ketoacyl-CoA thiolase and thereby fatty acid oxidation in rat liver mitochondria

Biochemistry ◽  
1988 ◽  
Vol 27 (16) ◽  
pp. 5995-6000 ◽  
Author(s):  
Jianxun Li ◽  
Horst Schulz

FEBS Letters ◽  
1999 ◽  
Vol 460 (2) ◽  
pp. 241-245 ◽  
Author(s):  
Peter Turkaly ◽  
Janos Kerner ◽  
Charles Hoppel


1983 ◽  
Vol 141 (1) ◽  
pp. 33-39 ◽  
Author(s):  
NOBUHIRO MORISAKI ◽  
NOBUO MATSUOKA ◽  
YASUSHI SAITO ◽  
AKIRA KUMAGAI


1972 ◽  
Vol 25 (9) ◽  
pp. 681-685
Author(s):  
Misako Taniguchi ◽  
Ryoko Yamauchi ◽  
Motoomi Nakamura




1981 ◽  
Vol 200 (2) ◽  
pp. 217-223 ◽  
Author(s):  
J D McGarry ◽  
D W Foster

The experiments reconfirm the powerful inhibitory effect of malonyl-CoA on carnitine acyltransferase I and fatty acid oxidation in rat liver mitochondria (Ki 1.5 microM). Sensitivity decreased with starvation (Ki after 18 h starvation 3.0 microM, and after 42 h 5.0 microM). Observations by Cook, Otto & Cornell [Biochem. J. (1980) 192, 955--958] and Ontko & Johns [Biochem. J. (1980) 192, 959--962] have cast doubt on the physiological role of malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis. The high Ki values obtained in the cited studies are shown to be due to incubation conditions that cause substrate depletion, destruction of malonyl-CoA or generation of excessively high concentrations of unbound acyl-CoA (which offsets the competitive inhibition of malonyl-CoA towards carnitine acyltransferase I). The present results are entirely consistent with the postulated role of malonyl-CoA as the primary regulatory of fatty acid synthesis and oxidation in rat liver.



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