Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelet?

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Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelet?

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. Separation from nonspecific acyl-CoA synthetase and distribution in various cells and tissues.

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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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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The microsomal dicarboxylyl-CoA synthetase.

Dicarboxylic acids are products of the omega-oxidation of monocarboxylic acids. We demonstrate that in rat liver dicarboxylic acids (C5-C16) can be converted into their CoA esters by a dicarboxylyl-CoA synthetase. During this activation ATP, which cannot be replaced by GTP, is converted into AMP and PPi, both acting as feedback inhibitors of the reaction. Thermolabile at 37 degrees C, and optim...

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The Crystal Structure of Succinyl-CoA Synthetase

The x-ray crystal structure of succinyl-CoA synthetase (SCS) from Escherichia coli has been determined by the method of mu!tiple isomorphous replacement to a resolution of 2.5 A. Crystals of SCS are tetragonal with a space group of P4,22 oand unit cell dimensions of a = b = 98.47 A and c = 400.6 A. One molecule of SCS (142 kDa) is contained in the asymmetric unit. The current model has been ref...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1991

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2740145