| pubmed-article:10212254 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10212254 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:10212254 | lifeskim:mentions | umls-concept:C0752063 | lld:lifeskim |
| pubmed-article:10212254 | lifeskim:mentions | umls-concept:C0050690 | lld:lifeskim |
| pubmed-article:10212254 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:10212254 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:10212254 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:10212254 | pubmed:dateCreated | 1999-6-3 | lld:pubmed |
| pubmed-article:10212254 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10212254 | pubmed:abstractText | Short-chain acyl-CoA oxidases are beta-oxidation enzymes that are active on short-chain acyl-CoAs and that appear to be present in higher plant peroxisomes and absent in mammalian peroxisomes. Therefore, plant peroxisomes are capable of performing complete beta-oxidation of acyl-CoA chains, whereas mammalian peroxisomes can perform beta-oxidation of only those acyl-CoA chains that are larger than octanoyl-CoA (C8). In this report, we have shown that a novel acyl-CoA oxidase can oxidize short-chain acyl-CoA in plant peroxisomes. A peroxisomal short-chain acyl-CoA oxidase from Arabidopsis was purified following the expression of the Arabidopsis cDNA in a baculovirus expression system. The purified enzyme was active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Cell fractionation and immunocytochemical analysis revealed that the short-chain acyl-CoA oxidase is localized in peroxisomes. The expression pattern of the short-chain acyl-CoA oxidase was similar to that of peroxisomal 3-ketoacyl-CoA thiolase, a marker enzyme of fatty acid beta-oxidation, during post-germinative growth. Although the molecular structure and amino acid sequence of the enzyme are similar to those of mammalian mitochondrial acyl-CoA dehydrogenase, the purified enzyme has no activity as acyl-CoA dehydrogenase. These results indicate that the short-chain acyl-CoA oxidases function in fatty acid beta-oxidation in plant peroxisomes, and that by the cooperative action of long- and short-chain acyl-CoA oxidases, plant peroxisomes are capable of performing the complete beta-oxidation of acyl-CoA. | lld:pubmed |
| pubmed-article:10212254 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10212254 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10212254 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10212254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10212254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10212254 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10212254 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10212254 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10212254 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10212254 | pubmed:author | pubmed-author:NishimuraMM | lld:pubmed |
| pubmed-article:10212254 | pubmed:author | pubmed-author:HayashiHH | lld:pubmed |
| pubmed-article:10212254 | pubmed:author | pubmed-author:HayashiMM | lld:pubmed |
| pubmed-article:10212254 | pubmed:author | pubmed-author:KondoMM | lld:pubmed |
| pubmed-article:10212254 | pubmed:author | pubmed-author:CiurloGG | lld:pubmed |
| pubmed-article:10212254 | pubmed:author | pubmed-author:De BellisLL | lld:pubmed |
| pubmed-article:10212254 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10212254 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:10212254 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10212254 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10212254 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10212254 | pubmed:pagination | 12715-21 | lld:pubmed |
| pubmed-article:10212254 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10212254 | pubmed:meshHeading | pubmed-meshheading:10212254... | lld:pubmed |
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| pubmed-article:10212254 | pubmed:meshHeading | pubmed-meshheading:10212254... | lld:pubmed |
| pubmed-article:10212254 | pubmed:meshHeading | pubmed-meshheading:10212254... | lld:pubmed |
| pubmed-article:10212254 | pubmed:meshHeading | pubmed-meshheading:10212254... | lld:pubmed |
| pubmed-article:10212254 | pubmed:meshHeading | pubmed-meshheading:10212254... | lld:pubmed |
| pubmed-article:10212254 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10212254 | pubmed:articleTitle | A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. | lld:pubmed |
| pubmed-article:10212254 | pubmed:affiliation | Department of Cell Biology, National Institute for Basic Biology, Graduate University for Advanced Studies, Okazaki 444-8585, Japan. | lld:pubmed |
| pubmed-article:10212254 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10212254 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:824347 | entrezgene:pubmed | pubmed-article:10212254 | lld:entrezgene |
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