Palmityl coenzyme A deacylase.
نویسندگان
چکیده
Several different enzymes have been described which catalyze hydrolysis of acyl CoA derivatives. Acetyl CoA deacylase z, and succinyl CoA deacylase z-4, hydroxyisobutyryl CoA deaeylase ~ and a hydroxymethyl glutaryl CoA deacylase 6 have been described. Enzyme preparations that deacylate acetoacetyl CoA have been described~, 8 but recent evidence points to a more involved mechanism than one of simple hydrolysis 9, lO In addition, cleavage of long chain fatty acyl glutathione compounds have been reported u, 13. PORTER AND TIETZ and PORTER AND LONG have reported the presence of palmityl CoA deacylase ill pigeon liver 13,14. The purpose of this paper is to present an isolation procedure and several assay methods for a long chain fatty acyl CoA deacylase found in pig brain.
منابع مشابه
Functional deacylases of pigeon liver fatty acid synthetase complex.
Fatty acid synthetase complex (Mr = 500,000) purified from pigeon liver homogenates is inactivated by phenylmethylsulfonyl fluoride. A well characterized inhibitor of serine esterases. Pseudounimolecular kinetics are followed at all inhibitor concentrations studied (0.05 to 1.0 mM). The second order rate constant obtained at pH 7.0, 30 degrees in 0.05 M potassium phosphate, 1 mM EDTA is 250 plu...
متن کاملThe mechanism of substrate inhibition of palmityl coenzyme A:carnitine palmityltransferase by palmityl coenzyme A.
The substrate inhibition of palmityl coenzyme A:carnitine 0-palmityltransferase (EC 2.3.1.-) by palmityl-CoA has been studied. Beside being a substrate for the enzyme, palmityl-CoA was found to behave as a competitive inhibitor for the second substrate (carnitine). The Ki was found to be approximately 3 X 10-e M, while the K, for palmityl-CoA was found to be approximately 10M5 M. Thus, the affi...
متن کاملStudies on acetyl-coenzyme A synthetase of yeast: inhibition by long-chain acyl-coenzyme A esters.
Long-chain acyl-coenzyme A (CoA) compounds (palmityl, stearyl, and oleyl) were found to be potent inhibitors of acetyl-CoA synthetase (ACS) of Saccharomyces cerevisiae strain LK2G12 from aerobic, but not from nonaerobic, cells. The effectiveness of the inhibitors of the aerobic enzyme was in the following order: palmityl-CoA < stearyl-CoA < oleyl-CoA. Short-chain acyl-CoA compounds (propionyl, ...
متن کاملLong-chain Carnitine Acyltransferase and the Role of Acylcarnitine Derivatives in the Catalytic Increase of Fatty Acid Oxidation Induced by Carnitine.
Carnitine-H3 or palmitate-U4 incubated with heart muscle preparations waa incorporated into a compound that had chromatographic behavior in several systems identical to that of palmitylcarnitine chemically synthesized from palmityl chloride and carnitine. Palmitylcarnitine biosynthesis from palmitic acid and carnitine was dependent upon ATP and CoA in addition to substrates and an enzyme prepar...
متن کاملLong-chain carnitine acyltransferase and the role of acylcarnitine derivatives in the catalytic increase
Carnitine-H3 or palmitate-U4 incubated with heart muscle preparations waa incorporated into a compound that had chromatographic behavior in several systems identical to that of palmitylcarnitine chemically synthesized from palmityl chloride and carnitine. Palmitylcarnitine biosynthesis from palmitic acid and carnitine was dependent upon ATP and CoA in addition to substrates and an enzyme prepar...
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ورودعنوان ژورنال:
- Biochimica et biophysica acta
دوره 33 2 شماره
صفحات -
تاریخ انتشار 1959