The source of malonyl-CoA in rat heart The calcium paradox releases acetyl-CoA carboxylase and not propionyl-CoA carboxylase
| Autor: | I. E. M. Luyt-Houwen, Hans R. Scholte, Willem C. Huismann, Marie-Louise Dubelaar |
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| Jazyk: | angličtina |
| Předmět: |
Male
Methylmalonyl-CoA Decarboxylase Carboxy-Lyases Biophysics Propionyl-CoA carboxylase Acetyl-CoA carboxylase Biochemistry Ligases chemistry.chemical_compound Structural Biology Methylcrotonyl-CoA carboxylase Carnitine Genetics medicine Animals Molecular Biology ACACB Carnitine O-Palmitoyltransferase Myocardium Rats Inbred Strains Cell Biology Calcium paradox Pyruvate carboxylase Rats Malonyl-CoA Propionyl-CoA carboxylase Malonyl Coenzyme A Malonyl-CoA chemistry (Rat heart) Carnitine palmitoyltransferase I Calcium Acyl Coenzyme A medicine.drug |
| Zdroj: | FEBS Letters. (1):47-50 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(86)81182-6 |
| Popis: | The formation of malonyl-CoA in rat heart is catalyzed by cytosolic acetyl-CoA carboxylase. The existence of this enzyme in heart is difficult to prove by the abundant occurrence of mitochondrial propionyl-CoA carboxylase, which is also able to catalyze the carboxylation of acetyl-CoA. We used the calcium paradox as a tool to separate cytosolic components from the remaining heart, and found that acetyl-CoA carboxylase activity was preferentially released, like lactate dehydrogenase and carnitine, while propionyl-CoA carboxylase was almost fully retained. Acetyl-CoA carboxylase activity was determined after activation by citrate ion and Mg2+. The activity decreased to 64% by 48 h of fasting. |
| Databáze: | OpenAIRE |
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