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IDI2, a Second Isopentenyl Diphosphate Isomerase in Mammals
We recently described the identification of a novel isopentenyl diphosphate isomerase, IDI2 in humans and mice. Our current data indicate that, in humans, IDI2 is expressed only in skeletal muscle. Expression constructs of human IDI2 in Saccharomyces cerevisiae can complement isomerase function in a...
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Published in: | The Journal of biological chemistry 2007-03, Vol.282 (9), p.6668-6676 |
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container_end_page | 6676 |
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container_title | The Journal of biological chemistry |
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creator | Clizbe, Daun B. Owens, Michelle L. Masuda, Kimberly R. Shackelford, Janis E. Krisans, Skaidrite K. |
description | We recently described the identification of a novel isopentenyl diphosphate isomerase, IDI2 in humans and mice. Our current data indicate that, in humans, IDI2 is expressed only in skeletal muscle. Expression constructs of human IDI2 in Saccharomyces cerevisiae can complement isomerase function in an idi1-deficient yeast strain. Furthermore, IDI2 has the ability to catalyze the isomerization of [14C]IPP to [14C]DMAPP. Enzyme kinetic analysis of partially purified IDI2 demonstrate the novel isozyme has a maximal relative specific activity of 1.2 × 10-1 ± 0.3 μmol min-1 mg-1 at pH 8.0 with a KIPPm value of 22.8 μm IPP. Both isozymes, IDI1 and IDI2 are localized to the peroxisome by a PTS1-dependent pathway. Finally, our data suggest that IDI2 is regulated independently from IDI1, by a mechanism that may involve PPARα. |
doi_str_mv | 10.1074/jbc.M610922200 |
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Our current data indicate that, in humans, IDI2 is expressed only in skeletal muscle. Expression constructs of human IDI2 in Saccharomyces cerevisiae can complement isomerase function in an idi1-deficient yeast strain. Furthermore, IDI2 has the ability to catalyze the isomerization of [14C]IPP to [14C]DMAPP. Enzyme kinetic analysis of partially purified IDI2 demonstrate the novel isozyme has a maximal relative specific activity of 1.2 × 10-1 ± 0.3 μmol min-1 mg-1 at pH 8.0 with a KIPPm value of 22.8 μm IPP. Both isozymes, IDI1 and IDI2 are localized to the peroxisome by a PTS1-dependent pathway. 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subjects | Animals Carbon-Carbon Double Bond Isomerases - genetics Carbon-Carbon Double Bond Isomerases - metabolism Catalysis Cloning, Molecular Genetic Complementation Test Hemiterpenes Humans Isoenzymes Isomerism Kinetics Mice Peroxisomes - enzymology PPAR alpha Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics |
title | IDI2, a Second Isopentenyl Diphosphate Isomerase in Mammals |
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