Activation of Phosphoenolpyruvate Carboxylase from Escherichia coli by Long-Chain Acyl Derivatives of Coenzyme A and by Blue Dextran 2000

1978 ◽  
Vol 6 (1) ◽  
pp. 182-184 ◽  
Author(s):  
MICHAEL C. SCRUTTON
Keyword(s):  
Escherichia Coli ◽  
Phosphoenolpyruvate Carboxylase ◽  
Coenzyme A ◽  
Blue Dextran ◽  
Chain Acyl ◽  
Derivatives Of ◽  
Acyl Derivatives ◽  
Long Chain

scholarly journals Mechanism of the control of (Na+ + K+)-ATPase by long-chain acyl coenzyme A

1989 ◽  
Vol 264 (5) ◽  
pp. 2605-2608
Author(s):  
W H Huang ◽  
Y Wang ◽  
A Askari
Keyword(s):  
Coenzyme A ◽  
Chain Acyl ◽  
Acyl Coenzyme A ◽  
Long Chain

Stimulation of myocardial coenzyme A degradation by fatty acids

1987 ◽  
Vol 253 (1) ◽  
pp. H41-H46
Author(s):  
G. D. Lopaschuk ◽  
J. R. Neely
Keyword(s):  
Fatty Acids ◽  
Coenzyme A ◽  
Future Studies ◽  
Isolated Hearts ◽  
Tissue Content ◽  
Chain Acyl ◽  
Long Chain ◽  
Stimulation Of

Coenzyme A (CoA) levels were increased in isolated hearts from 537 +/- 14 to 818 +/- 44 nmol/g dry wt by perfusion for 45 min under conditions known to stimulate CoA synthesis (5). Subsequently, perfusion of these hearts with buffer containing glucose (11 mM) and pyruvate (5 mM) for 3 min had no effect on CoA levels (789 +/- 42 nmol/g dry wt). However, perfusion with a buffer containing glucose (11 mM) and palmitate (1.2 mM) decreased CoA levels to 683 +/- 34 nmol/g dry wt within 3 min. This decrease in CoA appeared to occur in the cytosolic compartment with no change in mitochondrial CoA content and was associated with a rise in tissue content of long-chain acyl-CoA. An increased incorporation of fatty acids into triglycerides was associated with the rise in total acyl-CoA suggesting that long-chain acyl-CoA levels were elevated in the cytosolic compartment. Perfusion conditions which maximally increased acyl-CoA levels also maximally stimulated CoA degradation. These observations suggest that the cytosolic degradation of CoA is related to high levels of long-chain acyl-CoA in this compartment. Use of these perfusion conditions in future studies should help define the pathway of CoA degradation and determine the mechanisms which control cellular levels of CoA.

ANALYSIS OF LONG-CHAIN ACYL-COENZYME A ESTERS

2012 ◽  
pp. 109-131 ◽  
Author(s):  
Tine Bækdal ◽  
Charlotte Karlskov Schjerling ◽  
Jan Krogh Hansen ◽  
Jens Knudsen
Keyword(s):  
Coenzyme A ◽  
Chain Acyl ◽  
Acyl Coenzyme A ◽  
Coenzyme A Esters ◽  
Long Chain

Very long-chain acyl coenzyme A dehydrogenase deficiency presenting with exercise-induced myoglobinuria

Neurology ◽  
1994 ◽  
Vol 44 (3, Part 1) ◽  
pp. 467-467 ◽  
Author(s):  
I. Ogilvie ◽  
M. Pourfarzam ◽  
S. Jackson ◽  
C. Stockdale ◽  
K. Bartlett ◽  
...  
Keyword(s):  
Dehydrogenase Deficiency ◽  
Coenzyme A ◽  
Chain Acyl ◽  
Exercise Induced ◽  
Acyl Coenzyme A ◽  
Long Chain

The lipase activity of a partially purified lipolytic enzyme of Escherichia coli

1978 ◽  
Vol 56 (5) ◽  
pp. 324-328 ◽  
Author(s):  
G. Nantel ◽  
Georgia Baraff ◽  
P. Proulx
Keyword(s):  
Escherichia Coli ◽  
Lipase Activity ◽  
Slow Rate ◽  
Water Soluble ◽  
Lipolytic Enzyme ◽  
Ph Optimum ◽  
Chain Acyl ◽  
Marked Preference ◽  
Hydrolysis Of ◽  
Long Chain

Escherichia coli lipase was found to have a broad pH optimum between pH 8 and 10. Long-chain acyl triacylglycerols such as trioleoylglycerol were hydrolysed at a relatively slow rate, whereas, the shorter-chain acyl derivative tricapryloylglycerol was not. Triacylglycerols and diacylglycerols were broken down at a rate 10- to 15-fold greater than that for monoacylglycerol. Simple esters such as methyloieate and cetylpalmitate were hydrolysed at rates greater than that of triacylglycerol. Water-soluble esters such as p-nitrophenylacetate were not attacked. Hydrolysis of lipase substrates occurred more readily in the presence of an anionic detergent such as taurocholate. The enzyme had no marked preference for the 1- or 3-position of triacylglycerols but attacked these positions much more readily than position 2. The enzyme also catalyzed transacylation reactions with simple alcohols such as methanol or ethanol.

Sign in / Sign up

Export Citation Format

Share Document