Identification of possible intermediates in the mitochondrial fatty acid chain elongation system

Biochemistry ◽  
1970 ◽  
Vol 9 (10) ◽  
pp. 2143-2152 ◽  
Author(s):  
Edward J. Barron ◽  
Larry A. Mooney
Keyword(s):  
Fatty Acid ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Mitochondrial Fatty Acid

scholarly journals Inhibition of rat liver microsomal fatty acid chain elongation by gemfibrozil in vitro

FEBS Letters ◽  
1992 ◽  
Vol 300 (1) ◽  
pp. 89-92 ◽  
Author(s):  
R.M. Sánchez ◽  
M. Viñals ◽  
M. Alegret ◽  
M. Vázquez ◽  
T. Adzet ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Rat Liver ◽  
Chain Elongation ◽  
Fatty Acid Chain

Reduced activity of hepatic microsomal fatty acid chain elongation synthesis in clofibrate-fed rats

1977 ◽  
Vol 26 (15) ◽  
pp. 1401-1404 ◽  
Author(s):  
Clemente Landriscina ◽  
Francesca M. Ruggiero ◽  
Gabriele V. Gnoni ◽  
Ernesto Quagliariello
Keyword(s):  
Fatty Acid ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Reduced Activity

scholarly journals Microbial Type I Fatty Acid Synthases (FAS): Major Players in a Network of Cellular FAS Systems

2004 ◽  
Vol 68 (3) ◽  
pp. 501-517 ◽  
Author(s):  
Eckhart Schweizer ◽  
Jörg Hofmann
Keyword(s):  
Fatty Acid ◽  
De Novo ◽  
Acid Synthesis ◽  
Chain Elongation ◽  
Type I ◽  
Mitochondrial Fatty Acid ◽  
Fatty Acid Synthases ◽  
Single Polypeptide ◽  
The Individual ◽  
Targeted Inactivation

SUMMARY The present review focuses on microbial type I fatty acid synthases (FASs), demonstrating their structural and functional diversity. Depending on their origin and biochemical function, multifunctional type I FAS proteins form dimers or hexamers with characteristic organization of their catalytic domains. A single polypeptide may contain one or more sets of the eight FAS component functions. Alternatively, these functions may split up into two different and mutually complementing subunits. Targeted inactivation of the individual yeast FAS acylation sites allowed us to define their roles during the overall catalytic process. In particular, their pronounced negative cooperativity is presumed to coordinate the FAS initiation and chain elongation reactions. Expression of the unlinked genes, FAS1 and FAS2, is in part constitutive and in part subject to repression by the phospholipid precursors inositol and choline. The interplay of the involved regulatory proteins, Rap1, Reb1, Abf1, Ino2/Ino4, Opi1, Sin3 and TFIIB, has been elucidated in considerable detail. Balanced levels of subunits α and β are ensured by an autoregulatory effect of FAS1 on FAS2 expression and by posttranslational degradation of excess FAS subunits. The functional specificity of type I FAS multienzymes usually requires the presence of multiple FAS systems within the same cell. De novo synthesis of long-chain fatty acids, mitochondrial fatty acid synthesis, acylation of certain secondary metabolites and coenzymes, fatty acid elongation, and the vast diversity of mycobacterial lipids each result from specific FAS activities. The microcompartmentalization of FAS activities in type I multienzymes may thus allow for both the controlled and concerted action of multiple FAS systems within the same cell.

scholarly journals The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

1976 ◽  
Vol 160 (2) ◽  
pp. 247-251 ◽  
Author(s):  
P J Brophy ◽  
D E Vance
Keyword(s):  
Fatty Acid ◽  
Microsomal Fraction ◽  
Specific Activity ◽  
Arachidic Acid ◽  
Fatty Acyl ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Specific Activities ◽  
Coa Hydrolase ◽  
Long Chain

1. The specific activities of long-chain fatty acid-CoA ligase (EC6.2.1.3) and of long-chain fatty acyl-CoA hydrolase (EC3.1.2.2) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids.

Fibrates modify rat hepatic fatty acid chain elongation and desaturation in vitro

1993 ◽  
Vol 46 (10) ◽  
pp. 1791-1796 ◽  
Author(s):  
Rosa M. Sánchez ◽  
Marisa Viñals ◽  
Marta Alegret ◽  
Manuel Vázquez ◽  
Tomás Adzet ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Chain Elongation ◽  
Hepatic Fatty Acid ◽  
Fatty Acid Chain
Sign in / Sign up

Export Citation Format

Share Document