Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 17-25 |
| Number of pages | 9 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 472 |
| Issue number | 1 |
| DOIs | |
| State | Published - Apr 1 2008 |
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Keywords
- β-Oxidation
- Compartmentalization
- Isocitrate dehydrogenase
- NADPH
- Saccharomyces cerevisiae
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Dual compartmental localization and function of mammalian NADP+-specific isocitrate dehydrogenase in yeast. / Lu, Qian; Minard, Karyl I.; McAlister-Henn, Lee.
In: Archives of Biochemistry and Biophysics, Vol. 472, No. 1, 01.04.2008, p. 17-25.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dual compartmental localization and function of mammalian NADP+-specific isocitrate dehydrogenase in yeast
AU - Lu, Qian
AU - Minard, Karyl I.
AU - McAlister-Henn, Lee
PY - 2008/4/1
Y1 - 2008/4/1
N2 - 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.
AB - 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.
KW - β-Oxidation
KW - Compartmentalization
KW - Isocitrate dehydrogenase
KW - NADPH
KW - Saccharomyces cerevisiae
UR - http://www.scopus.com/inward/record.url?scp=40649125743&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=40649125743&partnerID=8YFLogxK
U2 - 10.1016/j.abb.2008.01.025
DO - 10.1016/j.abb.2008.01.025
M3 - Article
VL - 472
SP - 17
EP - 25
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -