Long-chain-acyl-CoA synthetase activities in peroxisomes and microsomes from rat liver. An enzymological study
نویسندگان
چکیده
منابع مشابه
Phytanic acid activation in rat liver peroxisomes is catalyzed by long-chain acyl-CoA synthetase.
In Refsum disease, disorders of peroxisome biogenesis, and rhizomelic chondrodysplasia punctata, pathological accumulation of phytanic acid results from impaired alpha-oxidation of this branched-chain fatty acid. Previous studies from this laboratory indicated that activation of phytanic acid to its CoA derivative precedes its alpha-oxidation in peroxisomes. It was reported that this reaction i...
متن کاملStructure and regulation of rat long-chain acyl-CoA synthetase.
Complementary DNAs encoding rat long-chain acyl-CoA synthetase have been isolated. The cDNAs were identified using synthetic oligonucleotide probes based on partial amino acid sequences of lysyl endopeptidase peptides of the purified enzyme. Rat long-chain acyl-CoA synthetase is predicted to contain 699 amino acid residues and to have a calculated molecular weight of 78,177. Significant sequenc...
متن کاملKinetic studies on the chain length specificity of long chain acyl coenzyme A synthetase from rat liver microsomes.
The kinetics of activation of saturated fatty acids by long chain acyl-CoA synthetase from rat liver microsomes has been studied with a method of selective extraction of free fatty acids based on the insolubility of acyl-CoA in diethyl ether. Saturated fatty acids with a chain length ranging from Cl* to Co were assayed at concentrations varying from 0.5 to 10 PM. Under these conditions, Vm,, is...
متن کاملCloning and characterization of a hormonally regulated rat long chain acyl-CoA synthetase.
A previously unidentified gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) was cloned and characterized as a 79-kDa cytoplasmic protein expressed in Leydig cells of the rat testis. GR-LACS shares sequence identity with two conserved regions of the LACS and luciferase families, including the ATP/AMP binding domain and the 25-aa fatty acyl-CoA synthetase signature motif, but displa...
متن کاملReversible inactivation by noradrenaline of long-chain fatty acyl-CoA synthetase in rat adipocytes.
Incubation of rat adipocytes with the same range of noradrenaline concentrations that stimulate lipolysis caused a rapid and stable decrease in the activity of fatty acyl-CoA synthetase. Corticotropin, glucagon and dibutyryl cyclic AMP also decreased the activity of the enzyme. The effect of noradrenaline was apparent over a wide range of concentrations for the three substrates of the enzyme. A...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1991
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1991.tb15844.x