scholarly journals Acetate trafficking in the heart: carnitine acyltransferases matter

2016 ◽  
Vol 4 (19) ◽  
pp. e12997 ◽  
Author(s):  
Victor Zammit ◽  
Arduino Arduini
Keyword(s):  
Carnitine Acyltransferases

scholarly journals The Localization of Acyl Coenzyme A-Carnitine Acyltransferases in Rat Liver Cells

1967 ◽  
Vol 242 (3) ◽  
pp. 407-411
Author(s):  
Kaare R. Norum ◽  
Jon Bremer
Keyword(s):  
Rat Liver ◽  
Coenzyme A ◽  
Liver Cells ◽  
Rat Liver Cells ◽  
Carnitine Acyltransferases ◽  
Acyl Coenzyme A

Different carnitine acyltransferases in calf liver

1972 ◽  
Vol 280 (3) ◽  
pp. 422-433 ◽  
Author(s):  
Helge Erik Solberg
Keyword(s):  
Carnitine Acyltransferases

Carnitine acyltransferases in chloroplasts of Pisum sativum L.

Planta ◽  
1985 ◽  
Vol 163 (2) ◽  
pp. 197-200 ◽  
Author(s):  
I. McLaren ◽  
C. Wood ◽  
M. N. H. Jalil ◽  
B. C. S. Yong ◽  
D. R. Thomas
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L ◽  
Carnitine Acyltransferases

The Effect of Long-Term Fasting on the Branched Chain Acylcarnitines and Branched Chain Carnitine Acyltransferases

1979 ◽  
Vol 109 (1) ◽  
pp. 155-161 ◽  
Author(s):  
Y. R. Choi ◽  
P. J. Fogle ◽  
L. L. Bieber
Keyword(s):  
Carnitine Acyltransferases ◽  
Branched Chain

The Role of Carnitine Acyltransferases in the Maintenance of Cell Function

2005 ◽  
Vol 136 (8) ◽  
pp. 1299-1309 ◽  
Author(s):  
Victor A. Zammit ◽  
Nigel T. Price ◽  
Vicky N. Jackson ◽  
Byun-Sung Park
Keyword(s):  
Cell Function ◽  
Carnitine Acyltransferases

Inhibition of liver microsomal carnitine acyltransferases by sulphonylurea drugs

FEBS Letters ◽  
1995 ◽  
Vol 371 (2) ◽  
pp. 137-139 ◽  
Author(s):  
Neil M. Broadway ◽  
E.David Saggerson
Keyword(s):  
Carnitine Acyltransferases

Evidence for carnitine acyltransferases associated with rat heart microsomes

1978 ◽  
Vol 9 (10) ◽  
pp. 761-765 ◽  
Author(s):  
Patricia J. Fogle ◽  
Loran L. Bieber
Keyword(s):  
Rat Heart ◽  
Carnitine Acyltransferases

scholarly journals Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a reaction-intermediate analogue

1993 ◽  
Vol 294 (3) ◽  
pp. 645-651 ◽  
Author(s):  
N Nic a′ Bháird ◽  
G Kumaravel ◽  
R D Gandour ◽  
M J Krueger ◽  
R R Ramsay
Keyword(s):  
Active Sites ◽  
Random Order ◽  
Kinetic Mechanism ◽  
Product Inhibition ◽  
Binding Domains ◽  
Cell Compartments ◽  
Mitochondrial Inner Membrane ◽  
Kinetic Mechanisms ◽  
Carnitine Acyltransferases ◽  
Inhibition Studies

The carnitine acyltransferases contribute to the modulation of the acyl-CoA/CoA ratio in various cell compartments with consequent effects on many aspects of fatty acid metabolism. The properties of the enzymes are different in each location. The kinetic mechanisms and kinetic parameters for the carnitine acyltransferases purified from peroxisomes (COT) and from the mitochondrial inner membrane (CPT-II) were determined. Product-inhibition studies established that COT follows a rapid-equilibrium random-order mechanism, but CPT-II follows a strictly ordered mechanism in which acyl-CoA or CoA must bind before the carnitine substrate. Hemipalmitoylcarnitinium [(+)-HPC], a prototype tetrahedral intermediate analogue of the acyltransferase reaction, inhibits CPT-II 100-fold better than COT. (+)-HPC behaves as an analogue of palmitoyl-L-carnitine with COT. In contrast, with CPT-II(+)-HPC binds more tightly to the enzyme than do substrates or products, suggesting that it is a good model for the transition state and, unlike palmitoyl-L-carnitine, (+)-HPC can bind to the free enzyme. The data support the concept of three binding domains for the acyltransferases, a CoA site, an acyl site and a carnitine site. The CoA site is similar in COT and CPT-II, but there are distinct differences between the carnitine-binding site which may dictate the kinetic mechanism.

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