Self-protection of cytosolic malate dehydrogenase against oxidative stress in Arabidopsis
Plant malate dehydrogenase (MDH) isoforms are found in different cell compartments and
function in key metabolic pathways. It is well known that the chloroplastic NADP-dependent
MDH activities are strictly redox regulated and controlled by light. However, redox
dependence of other NAD-dependent MDH isoforms have been less studied. Here, we
show by in vitro biochemical characterization that the major cytosolic MDH isoform
(cytMDH1) is sensitive to H2O2 through sulfur oxidation of cysteines and methionines …
function in key metabolic pathways. It is well known that the chloroplastic NADP-dependent
MDH activities are strictly redox regulated and controlled by light. However, redox
dependence of other NAD-dependent MDH isoforms have been less studied. Here, we
show by in vitro biochemical characterization that the major cytosolic MDH isoform
(cytMDH1) is sensitive to H2O2 through sulfur oxidation of cysteines and methionines …
Self-protection of cytosolic malate dehydrogenase against oxidative stress in Arabidopsis.
Plant malate dehydrogenase (MDH) isoforms are found in different cell compartments and
function in key metabolic pathways. It is well known that the chloroplastic NADP-dependent
MDH activities are strictly redox regulated and controlled by light. However, redox
dependence of other NAD-dependent MDH isoforms have been less studied. Here, we
show by in vitro biochemical characterization that the major cytosolic MDH isoform
(cytMDH1) is sensitive to H2O2 through sulfur oxidation of cysteines and methionines …
function in key metabolic pathways. It is well known that the chloroplastic NADP-dependent
MDH activities are strictly redox regulated and controlled by light. However, redox
dependence of other NAD-dependent MDH isoforms have been less studied. Here, we
show by in vitro biochemical characterization that the major cytosolic MDH isoform
(cytMDH1) is sensitive to H2O2 through sulfur oxidation of cysteines and methionines …
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