TY - JOUR
T1 - Molecular characterization of Saccharomyces cerevisiae Δ3,Δ2-enoyl- CoA isomerase
AU - Geisbrecht, Brian V.
AU - Zhu, Dai
AU - Schulz, Kerstin
AU - Nau, Katja
AU - Morrell, James C.
AU - Geraghty, Michael
AU - Schulz, Horst
AU - Erdmann, Ralf
AU - Gould, Stephen J.
PY - 1998/12/11
Y1 - 1998/12/11
N2 - We report here the identification of the Saccharomyces cerevisiae peroxisomal Δ3,Δ2-enoyl-CoA isomerase, an enzyme that is essential for the β-oxidation of unsaturated fatty acids. The yeast gene YLR284C was identified in an in silico screen for genes that contain an oleate response element, a transcription factor-binding site common to most fatty acid- induced genes. Growth on oleic acid resulted in a significant increase in YLR284C mRNA, demonstrating that it is indeed an oleate-induced gene. The deduced product of YLR284C contains a type 1 peroxisomal targeting signal- like sequence at its C terminus and localizes to the peroxisome in a PEX8- dependent manner. Removal of YLR284C from the S. cerevisiae genome eliminated growth on oleic acid, but had no effect on peroxisome biogenesis, indicating a role for YLR284C in fatty acid metabolism. Cells lacking YLR284C had no detectable Δ3,Δ2-enoyl-CoA isomerase activity, and a bacterially expressed form of this protein catalyzed the isomerization of 3-cis-octenoyl- CoA to 2-trans-octenoyl-CoA with a specific activity of 16 units/mg. We conclude that YLR284C encodes the yeast peroxisomal Δ3,Δ2-enoyl-CoA isomerase and propose a new name, ECI1, to reflect its enoyl-CoA isomerase activity.
AB - We report here the identification of the Saccharomyces cerevisiae peroxisomal Δ3,Δ2-enoyl-CoA isomerase, an enzyme that is essential for the β-oxidation of unsaturated fatty acids. The yeast gene YLR284C was identified in an in silico screen for genes that contain an oleate response element, a transcription factor-binding site common to most fatty acid- induced genes. Growth on oleic acid resulted in a significant increase in YLR284C mRNA, demonstrating that it is indeed an oleate-induced gene. The deduced product of YLR284C contains a type 1 peroxisomal targeting signal- like sequence at its C terminus and localizes to the peroxisome in a PEX8- dependent manner. Removal of YLR284C from the S. cerevisiae genome eliminated growth on oleic acid, but had no effect on peroxisome biogenesis, indicating a role for YLR284C in fatty acid metabolism. Cells lacking YLR284C had no detectable Δ3,Δ2-enoyl-CoA isomerase activity, and a bacterially expressed form of this protein catalyzed the isomerization of 3-cis-octenoyl- CoA to 2-trans-octenoyl-CoA with a specific activity of 16 units/mg. We conclude that YLR284C encodes the yeast peroxisomal Δ3,Δ2-enoyl-CoA isomerase and propose a new name, ECI1, to reflect its enoyl-CoA isomerase activity.
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U2 - 10.1074/jbc.273.50.33184
DO - 10.1074/jbc.273.50.33184
M3 - Article
C2 - 9837886
AN - SCOPUS:0032509340
SN - 0021-9258
VL - 273
SP - 33184
EP - 33191
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 50
ER -