The source of malonyl‐CoA in rat heart

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 c...

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Bibliographic Details
Published inFEBS letters Vol. 198; no. 1; pp. 47 - 50
Main Authors Scholte, Hans R., Luyt-Houwen, Inez E.M., Dubelaar, Marie-Louise, Huismann, Willem C.
Format Journal Article
LanguageEnglish
Published 17.03.1986
Subjects
Acetyl-CoA carboxylase
Calcium paradox
Carnitine palmitoyltransferase I
Malonyl-CoA Propionyl-CoA carboxylase
Rat heart
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)81182-6