Fatty acid structural requirements for activity of arachidonoyl-CoA synthetase.
نویسندگان
چکیده
منابع مشابه
Fatty acid structural requirements for activity of arachidonoyl-CoA synthetase.
We have examined the fatty acid substrate specificity of arachidonoyl-CoA synthetase from human platelet membranes. A variety of positional isomers and chain-length analogs of arachidonic acid [20:4(5, 8, 11, 14)] were synthesized, and assayed for their ability to inhibit arachidonoyl-CoA formation or to serve as substrates for the synthetase. The chain-length specificity of the synthetase for ...
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Apparent Km values have been determined for the substrates ATP, CoA and fatty acids for the long-chain acyl-CoA synthetase (EC 6.2.1.3) reaction in lysates of human blood platelets. The apparent Km for ATP was higher for saturated fatty acids (C12:0 to C18:0) than for unsaturated acids (C18:1 to C22:6). Other apparent Km values were very similar for all long-chain fatty acids tested. Palmitic a...
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Arachidonoyl-CoA synthetase was solubilized from a particulate fraction of calf brain and human platelets using 1% Nonidet P-40 and 10 mM EDTA. Arachidonoyl-CoA synthetase from both preparations was separated from nonspecific (long chain) acyl-CoA synthetase (EC 6.2.1.3) by chromatography on hydroxylapatite. To further substantiate that the two acyl-CoA synthetases are distinct proteins, we sol...
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The fatty acid (FA) degradation pathway of Pseudomonas aeruginosa, an opportunistic pathogen, was recently shown to be involved in nutrient acquisition during BALB/c mouse lung infection model. The source of FA in the lung is believed to be phosphatidylcholine, the major component of lung surfactant. Previous research indicated that P. aeruginosa has more than two fatty acyl-CoA synthetase gene...
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ژورنال
عنوان ژورنال: Journal of Lipid Research
سال: 1984
ISSN: 0022-2275
DOI: 10.1016/s0022-2275(20)37825-1