TY - JOUR
T1 - Characterization of PECL, a novel monofunctional δ3,δ2-enoyl-CoA isomerase of mammalian peroxisomes
AU - Geisbrecht, Brian V.
AU - Zhang, Dongyan
AU - Schulz, Horst
AU - Gould, Stephen J.
PY - 1999/7/30
Y1 - 1999/7/30
N2 - We report here the identification and characterization of human and mouse PECI, a novel gene that encodes a monofunctional peroxisomal Δ3,Δ2- enoyl-CoA isomerase. Human and mouse PECI were identified on the basis of their sequence similarity to Eci1p, a recently characterized peroxisomal Δ3,Δ2-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 Δ3,Δ1-enoyl-CoA isomerase in peroxisomal metabolism are discussed.
AB - We report here the identification and characterization of human and mouse PECI, a novel gene that encodes a monofunctional peroxisomal Δ3,Δ2- enoyl-CoA isomerase. Human and mouse PECI were identified on the basis of their sequence similarity to Eci1p, a recently characterized peroxisomal Δ3,Δ2-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 Δ3,Δ1-enoyl-CoA isomerase in peroxisomal metabolism are discussed.
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U2 - 10.1074/jbc.274.31.21797
DO - 10.1074/jbc.274.31.21797
M3 - Article
C2 - 10419495
AN - SCOPUS:0033618161
SN - 0021-9258
VL - 274
SP - 21797
EP - 21803
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 31
ER -