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Plant Physiol, June 2000, Vol. 123, pp. 733-742
ACX3, a Novel Medium-Chain Acyl-Coenzyme A Oxidase from
Arabidopsis
Byron E.
Froman,*
Patricia C.
Edwards,
Adam G.
Bursch, and
Katayoon
Dehesh
Calgene LLC, 1920 Fifth Street, Davis, California 95616
In a database search for homologs of acyl-coenzyme A oxidases (ACX)
in Arabidopsis, we identified a partial genomic sequence encoding an
apparently novel member of this gene family. Using this sequence
information we then isolated the corresponding full-length cDNA from
etiolated Arabidopsis cotyledons and have characterized the encoded
recombinant protein. The polypeptide contains 675 amino acids. The 34 residues at the amino terminus have sequence similarity to the
peroxisomal targeting signal 2 of glyoxysomal proteins, including the
R-[I/Q/L]-X5-HL-XL-X15-22-C consensus sequence, suggesting a possible
microsomal localization. Affinity purification of the encoded
recombinant protein expressed in Escherichia coli
followed by enzymatic assay, showed that this enzyme is active on C8:0-
to C14:0-coenzyme A with maximal activity on C12:0-coenzyme A,
indicating that it has medium-chain-specific activity. These data
indicate that the protein reported here is different from previously
characterized classes of ACX1, ACX2, and short-chain ACX (SACX), both
in sequence and substrate chain-length specificity profile. We
therefore, designate this new gene AtACX3. The temporal and spatial expression patterns of AtACX3 during
development and in various tissues were similar to those of the
AtSACX and other genes expressed in glyoxysomes.
Currently available database information indicates that
AtACX3 is present as a single copy gene.
*
Corresponding author; e-mail byron.froman{at}monsanto.com; fax
530-792-2453.
© 2000 American Society of Plant Physiologists
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