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J Biol Chem, Vol. 274, Issue 18, 12715-12721, April 30, 1999
A Novel Acyl-CoA Oxidase That Can Oxidize Short-chain Acyl-CoA in
Plant Peroxisomes
Hiroshi
Hayashi §,
Luigi
De Bellis ¶,
Adriana
Ciurli¶,
Maki
Kondo ,
Makoto
Hayashi §, and
Mikio
Nishimura §
From the Department of Cell Biology, National
Institute for Basic Biology and the § Department of
Molecular Biomechanics, Graduate University for Advanced Studies,
Okazaki 444-8585, Japan and the ¶ Dipartimento di Biologia delle
Piante Agrarie, via Mariscoglio 34, 56124 Pisa, Italy
Short-chain acyl-CoA oxidases are -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 -oxidation of acyl-CoA chains, whereas mammalian
peroxisomes can perform -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 -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 -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 -oxidation of
acyl-CoA.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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