Source:http://linkedlifedata.com/resource/pubmed/id/16476568
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2006-3-13
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pubmed:abstractText |
Acetate has been found as an endogenous metabolite of beta-oxidation of fatty acids in liver. In order to investigate the regulation of acetate generation in liver mitochondria, we attempted to purify a mitochondrial acetyl-CoA hydrolase in rat liver. This acetyl-CoA-hydrolyzing activity in isolated mitochondria was induced by the treatment of rats with di(2-ehtylhexyl)phthalate (DEHP), a peroxisome proliferator which induces expression of several peroxisomal and mitochondrial enzymes involved in beta-oxidation of fatty acids. The purified enzyme was 43-kDa in molecular mass by SDS/PAGE. Internal amino acid sequencing of this enzyme revealed that it was identical with mitochondrial 3-ketoacyl-CoA thiolase, suggesting that this enzyme has two kinds of activities, 3-ketoacyl-CoA thiolase and acetyl-CoA hydrolase activities. Kinetic studies clearly indicated that this enzyme had the both activities and each activity was inhibited by the substrates of the other activity, that is, 3-ketoacyl-CoA thiolase activity was inhibited by acetyl-CoA, on the other hand, acetyl-CoA hydrolase activity was inhibited by acetoacetyl-CoA in a competitive manner. These findings suggested that acetate generation in liver mitochondria is a side reaction of this known enzyme, 3-ketoacyl-CoA thiolase, and this enzyme may regulate its activities depending on each substrate level.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetates,
http://linkedlifedata.com/resource/pubmed/chemical/Acetyl-CoA C-Acyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Acetyl-CoA Hydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Diethylhexyl Phthalate
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1761
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16476568-Acetates,
pubmed-meshheading:16476568-Acetyl-CoA C-Acyltransferase,
pubmed-meshheading:16476568-Acetyl-CoA Hydrolase,
pubmed-meshheading:16476568-Acyl Coenzyme A,
pubmed-meshheading:16476568-Animals,
pubmed-meshheading:16476568-Chromatography, Gel,
pubmed-meshheading:16476568-Diethylhexyl Phthalate,
pubmed-meshheading:16476568-Enzyme Activation,
pubmed-meshheading:16476568-Kinetics,
pubmed-meshheading:16476568-Male,
pubmed-meshheading:16476568-Mitochondria, Liver,
pubmed-meshheading:16476568-Rats,
pubmed-meshheading:16476568-Rats, Sprague-Dawley
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pubmed:year |
2006
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pubmed:articleTitle |
Acetate generation in rat liver mitochondria; acetyl-CoA hydrolase activity is demonstrated by 3-ketoacyl-CoA thiolase.
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pubmed:affiliation |
Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University, 111 Kuboki, Soja-shi, Okayama 719-1197, Japan. yamashit@fhw.oka-pu.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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