Source:http://linkedlifedata.com/resource/pubmed/id/10212254
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1999-6-3
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pubmed:databankReference | |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12715-21
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10212254-Acyl-CoA Dehydrogenase,
pubmed-meshheading:10212254-Acyl-CoA Dehydrogenases,
pubmed-meshheading:10212254-Amino Acid Sequence,
pubmed-meshheading:10212254-Arabidopsis,
pubmed-meshheading:10212254-DNA, Complementary,
pubmed-meshheading:10212254-Microbodies,
pubmed-meshheading:10212254-Microscopy, Immunoelectron,
pubmed-meshheading:10212254-Molecular Sequence Data,
pubmed-meshheading:10212254-Oxidation-Reduction,
pubmed-meshheading:10212254-Sequence Homology, Amino Acid,
pubmed-meshheading:10212254-Substrate Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes.
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pubmed:affiliation |
Department of Cell Biology, National Institute for Basic Biology, Graduate University for Advanced Studies, Okazaki 444-8585, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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