title: IDI2, a second isopentenyl diphosphate isomerase in mammals.
abstract: 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 [(14)C]IPP to [(14)C]DMAPP. Enzyme kinetic analysis of partially purified IDI2 demonstrate the novel isozyme has a maximal relative specific activity of 1.2 x 10(-1) +/- 0.3 micromol min(-1) mg(-1) at pH 8.0 with a K(IPP)(m) value of 22.8 microm 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 PPARalpha.
authors.affiliation: Department of Biology, San Diego State University, San Diego, California 92182, USA.
authors.forename: Daun B
authors.initials: DB
authors.lastname: Clizbe
authors.forename: Michelle L
authors.initials: ML
authors.lastname: Owens
authors.forename: Kimberly R
authors.initials: KR
authors.lastname: Masuda
authors.forename: Janis E
authors.initials: JE
authors.lastname: Shackelford
authors.forename: Skaidrite K
authors.initials: SK
authors.lastname: Krisans
mesh_terms: D000818:Animals; D019748:Carbon-Carbon Double Bond Isomerases / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D003001:Cloning, Molecular; D005816:Genetic Complementation Test; D045782:Hemiterpenes; D006801:Humans; D007527:Isoenzymes; D007536:Isomerism; D007700:Kinetics; D051379:Mice; D047493:PPAR alpha; D020675:Peroxisomes / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000235:genetics
chemical_list: D045782:Hemiterpenes; D007527:Isoenzymes; D047493:PPAR alpha; D019748:Carbon-Carbon Double Bond Isomerases; C021453:isopentenyldiphosphate delta-isomerase