Fatty acid biosynthesis VII. Substrate control of chain-length of products synthesised by rat liver fatty acid synthetase

Author(s):  
H.J.M. Hansen ◽  
E.M. Carey ◽  
R. Dils
ChemBioChem ◽  
2019 ◽  
Vol 20 (18) ◽  
pp. 2298-2321 ◽  
Author(s):  
Christina S. Heil ◽  
S. Sophia Wehrheim ◽  
Karthik S. Paithankar ◽  
Martin Grininger

1980 ◽  
Vol 88 (2) ◽  
pp. 303-306 ◽  
Author(s):  
Akihiko KAWAGUCHI ◽  
Kazumi ARAI ◽  
Yousuke SEYAMA ◽  
Tamio YAMAKAWA ◽  
Shigenobu OKUDA

1990 ◽  
Vol 45 (5) ◽  
pp. 518-520 ◽  
Author(s):  
Manfred Focke ◽  
Andrea Feld ◽  
Hartmut K. Lichtenthaler

Thiolactomycin was shown to be a potent inhibitor of de novo fatty acid biosynthesis in intact isolated chloroplasts (measured as [14C]acetate incorporation into total fatty acids). In our attempt to further localize the inhibition site we confirmed the inhibition with a fatty acid synthetase preparation, measuring the incorporation of [14C]malonyl-CoA into total fatty acids. From the two proposed enzymic targets of the fatty acid synthetase by thiolactomycin we could exclude the acetyl-CoA: ACP transacetylase. It appears that the inhibition by thiolactomycin occurs on the level of the condensing enzymes, i.e. the 3-oxoacyl-ACP synthases. We also demonstrated that the two starting enzymes of de novo fatty acid biosynthesis, the acetyl-CoA synthetase and the acetyl-CoA carboxylase, are not affected by thiolactomycin.


1977 ◽  
Vol 183 (2) ◽  
pp. 710-717 ◽  
Author(s):  
Gary G. Shutle ◽  
John M. Langstaff ◽  
James C. Jamieson ◽  
David N. Burton

1984 ◽  
Vol 140 (2) ◽  
pp. 441-445 ◽  
Author(s):  
Carl M. NEPOKROEFF ◽  
Kazuo ADACHI ◽  
Chen YAN ◽  
John, W. PORTER

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