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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1989-1-4
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| pubmed:abstractText |
The present study was designed to determine the action of the 2-acetylenic acid thioester on mitochondrial fatty acid chain elongation and beta-oxidation. Addition of 2-decynoyl CoA to a rat liver mitochondrial suspension resulted in a significant stimulation of the rate of oxidation of NADPH and NADH. This enhanced oxidation rate was not due to the mitochondrial trans-2-enoyl CoA reductase-catalyzed conversion of the 2-acetylenic acid thioester to the saturated product, decanoate, as measured by gas-liquid chromatography. On the contrary, the mitochondrial trans-2-enoyl CoA reductase activity was markedly inhibited by the 2-acetylenic acid derivative, as evidenced by the decrease in the reduction of trans-2-decenoyl CoA to decanoic acid. Incubation of the mitochondrial fraction with either NADPH or NADH and 2-decynol CoA resulted in the gas chromatographic identification of three products: beta-ketodecanoate, beta-hydroxydecanoate, and trans-2-decenoate. In the absence of reduced pyridine nucleotide, a single product was formed and identified as beta-ketodecanoate. Confirmation of the identity of this product was obtained by the observation of the formation of the Mg2+-enolate complex (303-nm absorbance peak). These results suggest that, although the 2-decynoyl CoA is an inhibitor of mitochondrial trans-2-enoyl CoA reductase activity, it is a substrate for the mitochondrial trans-2-enoyl CoA hydratase (crotonase). This was confirmed by incubation of 2-decynoyl CoA with commercially purified liver mitochondrial crotonase. The beta-ketodecanoate is formed in a two-step process: hydration of the 2-decynoyl CoA to an unstable enol intermediate which undergoes rearrangement to the beta-ketodecanoyl CoA. Interestingly, although the mitochondrial crotonase can utilize the 2-acetylenic acid thioesters, this was not the case for the peroxisomal bifunctional hydratase which was markedly inhibited by varying concentrations of 2-decynoyl CoA.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-Hydroxyacyl CoA Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl-CoA Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Enoyl-CoA Hydratase,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Desaturases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/acetoacetyl-CoA reductase,
http://linkedlifedata.com/resource/pubmed/chemical/acyl-CoA dehydrogenase (NADP ),
http://linkedlifedata.com/resource/pubmed/chemical/dec-2-ynoyl-coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/peroxisomal-bifunctional enzyme
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0003-9861
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
267
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1-12
|
| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:3058034-3-Hydroxyacyl CoA Dehydrogenases,
pubmed-meshheading:3058034-Acyl Coenzyme A,
pubmed-meshheading:3058034-Acyl-CoA Dehydrogenases,
pubmed-meshheading:3058034-Alcohol Oxidoreductases,
pubmed-meshheading:3058034-Animals,
pubmed-meshheading:3058034-Catalysis,
pubmed-meshheading:3058034-Enoyl-CoA Hydratase,
pubmed-meshheading:3058034-Fatty Acid Desaturases,
pubmed-meshheading:3058034-Hydro-Lyases,
pubmed-meshheading:3058034-Isomerases,
pubmed-meshheading:3058034-Male,
pubmed-meshheading:3058034-Microbodies,
pubmed-meshheading:3058034-Microsomes, Liver,
pubmed-meshheading:3058034-Mitochondria, Liver,
pubmed-meshheading:3058034-Multienzyme Complexes,
pubmed-meshheading:3058034-NAD,
pubmed-meshheading:3058034-NADP,
pubmed-meshheading:3058034-Oxidation-Reduction,
pubmed-meshheading:3058034-Rats,
pubmed-meshheading:3058034-Rats, Inbred Strains,
pubmed-meshheading:3058034-Substrate Specificity
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| pubmed:year |
1988
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| pubmed:articleTitle |
Dual action of 2-decynoyl coenzyme A: inhibitor of hepatic mitochondrial trans-2-enoyl coenzyme A reductase and peroxisomal bifunctional protein and substrate for the mitochondrial beta-oxidation system.
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| pubmed:affiliation |
Department of Pharmacology, University of Connecticut Health Center, Farmington 06032.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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