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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1979-9-27
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pubmed:abstractText |
Biosynthesis of mevalonic acid (MVA), total formation of 14CO2 from [1,3-14C]malonyl-CoA and the activity of malonyl-CoA decarboxylase in subcellular fractions of rat liver were studied. The dependence of the rate of MVA biosynthesis on malonyl-CoA concentration was found to be linear both in 140,000 g supernatant and solubilized microsomal fractions. It was shown that in a composite system (140,000 g supernatant fraction added to washed microsomes, 10 : 1) the optimal concentration ratio for the substrates of MVA biosynthesis (malonyl-CoA and acetyl-CoA) is 1 to 2. In the absence of acetyl-CoA decarboxylation of [1,3-14C]malonyl-CoA was prevalent. In all subcellular fractions studied decarboxylation of [1,3-14C]malonyl-CoA prevailed over its incorporation into MVA, total non-saponified lipid fraction and fatty acids. The degree of malonyl-CoA, decarboxylation was not correlated with the rate of its incorporation into MVA, i. e. the increase in the 14CO2 formation was not accompanied by stimulation of [1,3-14C]malonyl-CoA incorporation either into MVA or into total non-saponified lipid fractions. The incorporation of [1-14C]acetyl-CoA into MVA under the same conditions was considerably lower than that of [1,3-14C]malonyl-CoA. In all subcellular fractions under study the activity of malonyl-CoA decarboxylase was found. The experimental data suggest that a remarkable part of malonyl-CoA is incorporated into MVA without preliminary decarboxylation. A possible role of malonyl-CoA decarboxylase as an enzyme which protects the cell against accumulation of malonyl-CoA and its immediate metabolites -- malonate and methylmalonyl-CoA is disucssed.
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pubmed:language |
rus
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxy-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Malonyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Mevalonic Acid
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0320-9725
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
851-63
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:454714-Acyl Coenzyme A,
pubmed-meshheading:454714-Animals,
pubmed-meshheading:454714-Carbon Dioxide,
pubmed-meshheading:454714-Carboxy-Lyases,
pubmed-meshheading:454714-Cytosol,
pubmed-meshheading:454714-Kinetics,
pubmed-meshheading:454714-Liver,
pubmed-meshheading:454714-Male,
pubmed-meshheading:454714-Malonyl Coenzyme A,
pubmed-meshheading:454714-Mevalonic Acid,
pubmed-meshheading:454714-Microsomes, Liver,
pubmed-meshheading:454714-Rats
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pubmed:year |
1979
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pubmed:articleTitle |
[Decarboxylation of malonyl-CoA and biosynthesis of mevalonic acid in rat liver].
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pubmed:publicationType |
Journal Article,
English Abstract
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