| pubmed-article:16476568 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16476568 | lifeskim:mentions | umls-concept:C0026239 | lld:lifeskim |
| pubmed-article:16476568 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:16476568 | lifeskim:mentions | umls-concept:C0001021 | lld:lifeskim |
| pubmed-article:16476568 | lifeskim:mentions | umls-concept:C0000975 | lld:lifeskim |
| pubmed-article:16476568 | lifeskim:mentions | umls-concept:C1149984 | lld:lifeskim |
| pubmed-article:16476568 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:16476568 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16476568 | pubmed:dateCreated | 2006-3-13 | lld:pubmed |
| pubmed-article:16476568 | 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. | lld:pubmed |
| pubmed-article:16476568 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16476568 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16476568 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16476568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16476568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16476568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16476568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16476568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16476568 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16476568 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16476568 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:16476568 | pubmed:author | pubmed-author:YamashitaHiro... | lld:pubmed |
| pubmed-article:16476568 | pubmed:author | pubmed-author:KimotoMasumiM | lld:pubmed |
| pubmed-article:16476568 | pubmed:author | pubmed-author:TsujiHideakiH | lld:pubmed |
| pubmed-article:16476568 | pubmed:author | pubmed-author:HiemoriMikiM | lld:pubmed |
| pubmed-article:16476568 | pubmed:author | pubmed-author:ItsukiAiA | lld:pubmed |
| pubmed-article:16476568 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16476568 | pubmed:volume | 1761 | lld:pubmed |
| pubmed-article:16476568 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16476568 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16476568 | pubmed:pagination | 17-23 | lld:pubmed |
| pubmed-article:16476568 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
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| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
| pubmed-article:16476568 | pubmed:meshHeading | pubmed-meshheading:16476568... | lld:pubmed |
| pubmed-article:16476568 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16476568 | pubmed:articleTitle | Acetate generation in rat liver mitochondria; acetyl-CoA hydrolase activity is demonstrated by 3-ketoacyl-CoA thiolase. | lld:pubmed |
| pubmed-article:16476568 | 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 | lld:pubmed |
| pubmed-article:16476568 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16476568 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:170465 | entrezgene:pubmed | pubmed-article:16476568 | lld:entrezgene |
| entrez-gene:170570 | entrezgene:pubmed | pubmed-article:16476568 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16476568 | lld:entrezgene |
