Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 472, Issue 1, Pages 17-25Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.01.025
Keywords
isocitrate dehydrogenase; Saccharomyces cerevisiae; compartmentalization; NADPH; beta-oxidation
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Funding
- NIA NIH HHS [R01 AG017477, R01 AG017477-08, AG17477] Funding Source: Medline
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Isozymes of NADP(+)-specific isocitrate dehydrogenase (IDP) provide NADPH in cytosolic, mitochondrial, and peroxisomal compartments of eukaryotic cells. Analyses of purified IDP isozymes from yeast and from mouse suggest a general correspondence of pH optima for catalysis and pI values with pH values reported for resident cellular compartments. However, mouse IDP2, which partitions between cytosolic and peroxisomal compartments in mammalian cells, exhibits a broad pH optimum and an intermediate pI value. Mouse IDP2 was found to similarly colocalize in both cellular compartments when expressed in yeast at levels equivalent to those of endogenous yeast isozymes. The mouse enzyme can compensate for loss of yeast cytosolic IDP2 and of peroxisomal IDP3. Removal of the peroxisomal targeting signal of the mouse enzyme precludes both localization in peroxisomes and compensation for loss of yeast IDP3. (c) 2008 Elsevier Inc. All rights reserved.
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