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J Biol Chem, Vol. 274, Issue 31, 21797-21803, July 30, 1999
3,
2-Enoyl-CoA Isomerase of Mammalian
Peroxisomes
,
From the We report here the identification and
characterization of human and mouse PECI, a novel gene that
encodes a monofunctional peroxisomal
Department of Biological Chemistry, The
Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205 and the § Department of
Chemistry, The City College of The City University of New York,
New York, 10031
3,
2-enoyl-CoA isomerase. Human and mouse
PECI were identified on the basis of their sequence
similarity to Eci1p, a recently characterized peroxisomal
3,
2-enoyl-CoA isomerase from the yeast
Saccharomyces cerevisiae. Cloning and sequencing of the
human PECI cDNA revealed the presence of a 1077-base
pair open reading frame predicted to encode a 359-amino acid protein
with a mass of 39.6 kDa. The corresponding mouse cDNA contains a
1074-base pair open reading frame that encodes a 358-amino acid-long
protein with a deduced mass of 39.4 kDa. Northern blot analysis
demonstrated human PECI mRNA is expressed in all
tissues. A bacterially expressed form of human PECI catalyzed the
isomerization of 3-cis-octenoyl-CoA to
2-trans-octenoyl-CoA with a specific activity of 27 units/mg of protein. The human and mouse PECI proteins contain type-1
peroxisomal targeting signals, and human PECI was localized to
peroxisomes by both subcellular fractionation and immunofluorescence
microscopy techniques. The potential roles for this monofunctional
3,
2-enoyl-CoA isomerase in peroxisomal
metabolism are discussed.
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