Deacylation of acetyl-coenzyme A and acetylcarnitine by liver preparations.
The breakdown of acetylcarnitine catalysed by extracts of rat and sheep liver was completely abolished by Sephadex G-25 gel filtration, whereas the hydrolysis of acetyl-CoA was unaffected. Acetyl-CoA and CoA acted catalytically in restoring the ability of Sephadex-treated extracts to break down acetylcarnitine, which was therefore not due to an acetylcarnitine hydrolase but to the sequential action of carnitine acetyltransferase and acetyl-CoA hydrolase. Some 75% of the acetyl-CoA hydrolase activity of sheep liver was localized in the mitochondrial fraction. Two distinct acetyl-CoA hydrolases were partially purified from extracts of sheep liver mitochondria. Both enzymes hydrolysed other short-chain acyl-CoA compounds and succinyl-CoA (3-carboxypropionyl-CoA), but with one acetyl-CoA was the preferred substrate.
D000085:Acetates / Q000378:metabolism; D000105:Acetyl Coenzyme A / Q000378:metabolism*; D000104:Acetyl-CoA Hydrolase / Q000378:metabolism; D000108:Acetylcarnitine / Q000378:metabolism*; D000818:Animals; D002331:Carnitine / Q000031:analogs & derivatives*; D002332:Carnitine O-Acetyltransferase / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology; D051381:Rats; D012756:Sheep
D000085:Acetates; D000108:Acetylcarnitine; D000105:Acetyl Coenzyme A; D002332:Carnitine O-Acetyltransferase; D000104:Acetyl-CoA Hydrolase; D002331:Carnitine