Pig Muscle Carnitine Palmitoyltransferase I (CPTIβ), with LowKmfor Carnitine and Low Sensitivity to Malonyl-CoA Inhibition, Has Kinetic Characteristics Similar to Those of the Rat Liver (CPTIα) Enzyme†

Biochemistry ◽  
2004 ◽  
Vol 43 (39) ◽  
pp. 12686-12691 ◽  
Author(s):  
Joana Relat ◽  
Carine Nicot ◽  
Mar Gacias ◽  
Gebre Woldegiorgis ◽  
Pedro F. Marrero ◽  
...  
2002 ◽  
Vol 278 (11) ◽  
pp. 9058-9063 ◽  
Author(s):  
Montserrat Morillas ◽  
Paulino Gómez-Puertas ◽  
Assia Bentebibel ◽  
Eva Sellés ◽  
Nuria Casals ◽  
...  

2002 ◽  
Vol 277 (49) ◽  
pp. 47184-47189 ◽  
Author(s):  
Yong Pan ◽  
Isabelle Cohen ◽  
Fanny Guillerault ◽  
Bruno Fève ◽  
Jean Girard ◽  
...  

1987 ◽  
Vol 243 (1) ◽  
pp. 261-265 ◽  
Author(s):  
B D Grantham ◽  
V A Zammit

The activation of overt carnitine palmitoyltransferase activity that occurs when rat liver mitochondria are incubated at near-physiological temperatures and ionic strengths was studied for mitochondria obtained from animals in different physiological states. In all instances, it was found to be due exclusively to an increase in the catalytic capacity of the enzyme and not to an increase in affinity of the enzyme for palmitoyl-CoA. The enzyme in mitochondria from fed animals always showed a larger degree of activation than that in mitochondria from starved animals. This was the case even for mitochondria (e.g. from fed diabetic animals) in which the kinetic characteristics of carnitine palmitoyltransferase were more similar to those for the enzyme in mitochondria from starved rats. Glucagon treatment of rats before isolation of the mitochondria did not affect the characteristics either of the kinetic parameters of overt carnitine palmitoyltransferase or of its activation in vitro.


1983 ◽  
Vol 214 (3) ◽  
pp. 1027-1030 ◽  
Author(s):  
V A Zammit

Preincubation of rat liver mitochondria with 5,5′-dithiobis-(2-nitrobenzoic acid) (Nbs2) followed by removal of excess reagent by washing the mitochondria with 0.5 mM-reduced glutathione resulted in a desensitization of carnitine palmitoyltransferase (CPT) I activity to malonyl-CoA inhibition. The effect was not observed if mitochondria were washed with 0.5 mM-dithiothreitol. The desensitization effect of Nbs2 could be reversed by a second incubation in the presence of 8 microM-malonyl-CoA. In addition, malonyl-CoA, when present simultaneously with Nbs2, protected CPT I activity against the desensitization effect of the thiol-group reagent. These results suggest that malonyl-CoA exerts an effect on one or more thiol groups of the enzyme, and that this effect is related to the ability of the metabolite to sensitize CPT I to malonyl-CoA inhibition.


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