Activation of hypolipidaemic drugs to acyl-coenzyme A thioesters
نویسندگان
چکیده
منابع مشابه
Synthesis of coenzyme A thioesters using methyl acyl phosphates in an aqueous medium.
Regioselective S-acylation of coenzyme A (CoA) is achieved under aqueous conditions using various aliphatic and aromatic carboxylic acids activated as their methyl acyl phosphate monoesters. Unlike many hydrophobic activating groups, the anionic methyl acyl phosphate mixed anhydride is more compatible with aqueous solvents, making it useful for conducting acylation reactions in an aqueous medium.
متن کاملThe crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioesters.
Synergistic investigations of the reactions catalyzed by several members of an enzyme superfamily provide a more complete understanding of the relationships between structure and function than is possible from focused studies of a single enzyme alone. The crotonase (or enoyl-CoA hydratase) superfamily is such an example whereby members catalyze a wide range of metabolic reactions but share a co...
متن کاملAcyl-coenzyme A synthetases.
The enzymes catalysing the initial stage of the 8-oxidation of fatty acids, the acyl-CoA synthetases, have been classified into four groups based on specificity. These are: the short-chain (acetyl-CoA synthetase; EC 6.2.1 .l), medium-chain (butyryl-CoA synthetase; EC 6.2.1.2) and the long-chain fatty acyl-CoA synthetase (acyl-CoA synthetase; EC 6.2.1.3), which are ATP-dependent and follow the r...
متن کاملFatty acyl-coenzyme A dehydrogenases.
Pande, S. V. & Parvin, R. (1976) J. Biol. Chem. 251,6683-6691 Pearson, D. J. & Tubbs, P. K. (1976) Biochem. J. 105,953-963 Ramsay, R. R. & Tubbs, P. K. (1974) Biochem. SOC. Traits. 2, 1285-1286 Ramsay, R. R. & Tubbs, P. K. (1975) FEBSLetf. 54,21-25 Ramsay, R. R. & Tubbs, P. K. (1976) Eur. J. Biochem. 69,299-303 Robles-Valdes, C . , McCarry, J. D. &Foster, D. W. (1976)J. Biol. Chern. 251, 6007-6...
متن کاملPositional specificities of acyl coenzyme A: glycerophosphate and acyl coenzyme A: monoacylglycerophosphate acyltransferases in Escherichia coli.
A particulate preparation isolated from Escherichia coli B catalyzes the acylation of 1-acyl-an-glycerol j-phosphate (I-acyl-GP) with both oleoyl-CoA and pahnitoyl-CoA. The optimum conditions were determined for the acyl-CoA: I-acyl-GP acyltransferase. The acyltransferase is specific for the I-acyl-GP and does not acylate 2-acyl-sn-glycerol 3-phosphate (2-acyl-GP) under the conditions used. The...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1986
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2390781