There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
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SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD+ oxidoreductase
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
isoforms cy MDH1 and cyMDH2 are reversibly inactivated by diamide treatment. Both NADH and GSH separately or together prevented inactivation of cyMDH1 and cyMDH2 by diamide
nuclear localization of cyMDH isoforms is significantly increased under oxidizing conditions in isolated Arabidopsis protoplasts, in particular of isoform cyMDH3
mMDH has a role in maximizing the photorespiratory rate. The slow-growing mmdh1mmdh2 mutant has elevated leaf respiration rate in the dark and light, without loss of photosynthetic capacity, suggesting that mMDH normally uses NADH to reduce oxaloacetate to malate, which is then exported to the cytosol, rather than to drive mitochondrial respiration. Increased respiratory rate in leaves can account in part for the low net CO2 assimilation and slow growth rate of mmdh1mmdh2. Loss of mMDH also affects photorespiration with alterations in CO2 assimilation/intercellular CO2 at low CO2, and the light-dependent elevated concentration of photorespiratory metabolites
a pdnad-mdh null mutation is embryo lethal. Plants with reduced pdNAD-MDH levels by means of artificial microRNA (miR-mdh-1) are viable, but dark metabolism is altered as reflected by increased nighttime malate, starch, and glutathione levels and a reduced respiration rate. pdNAD-MDH Silencing Results in small and pale green plants, phenotype, overvew. In addition, miR-mdh-1 plants exhibit strong pleiotropic effects, including dwarfism, reductions in chlorophyll levels, photosynthetic rate, and daytime carbohydrate levels, and disordered chloroplast ultrastructure, particularly in developing leaves, compared with the wild type. pdNAD-MDH deficiency in miR-mdh-1 can be functionally complemented by expression of a microRNA-insensitive pdNAD-MDH but not NADP-MDH, confirming distinct roles for NAD- and NADP-linked redox homeostasis
Arabidopsis enzyme knockout mutants are embryo-lethal, and a line with lowered enzyme from gene silencing has poor growth, pale leaves, disorganized chloroplasts, and low nighttime respiration
mMDH has a role in maximizing photorespiratory rate. The slow-growing mmdh1mmdh2 mutant has elevated leaf respiration rate in the dark and light, without loss of photosynthetic capacity, suggesting that mMDH normally uses NADH to reduce oxaloacetate to malate, which is then exported to the cytosol, rather than to drive mitochondrial respiration. Increased respiratory rate in leaves can account in part for the low net CO2 assimilation and slow growth rate of mmdh1mmdh2. Loss of mMDH also affects photorespiration with alterations in CO2 assimilation/intercellular CO2 at low CO2, and the light-dependent elevated concentration of photorespiratory metabolites
in illuminated chloroplasts, one mechanism involved in reduction-oxidation (redox) homeostasis is the malate-oxaloacetate shuttle. Excess electrons from photosynthetic electron transport in the form of nicotinamide adenine dinucleotide phosphate, reduced are used by NADP-dependent malate dehydrogenase (MDH), EC 1.1.1.82, to reduce oxaloacetate to malate, thus regenerating the electron acceptor NADP. NADP-MDH is a strictly redox-regulated, light-activated enzyme that is inactive in the dark. In the dark or in nonphotosynthetic tissues, the malate-oxaloacetate shuttle was proposed to be mediated by the constitutively active plastidial NAD-specific MDH isoform (pdNAD-MDH), but evidence is scarce. Critical role of pdNAD-MDH in Arabidopsis thaliana plants. Distinct roles for NAD- and NADP-linked redox homeostasis. pdNAD-MDH influences chloroplast ultrastructure and photosynthetic metabolism
the plastid-localized NAD-dependent MDH is important for plant survival in a dark or shady environment under which plNAD-MDH replaces the inactive chloroplast NADP-MDH in the regeneration of NAD+ to produce ATP
the enzyme is essential during embryogenesis and seed development. The protein, but not its NAD+-dependent malate dehydrogenase enzyme activity, is required for plastid development. The enzyme is required to stabilize filamentous temperature sensitive protease FtsH12
the enzyme is essential for early etioplast and chloroplast development due to its moonlighting role in stabilizing FtsH12, distinct from its enzymatic function
2 * 37000, SDS-PAGE. Thioredoxin-reversible homodimerization of isoform cytMDH1 through Cys330 disulfide formation protects the protein from overoxidation
purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of 0.0003 ml 6 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 200 mM NaCl, and 10% glycerol, with 0.0003 ml of reservoir solution containing 1.2 M sodium citrate tribasic dihydrate, pH 7.0, 20°C, method optimization, X-ray diffraction structure determination and analysis
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
the mutant of isoform cyMDH1 shows strongly decreased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
the mutant of isoform cyMDH1 shows slightly decreased activity compared to the wild type enzyme and is not inhibited by diamide. The mutant of isoform cyMDH2 shows decreased activity compared to the wild type enzyme and is not inhibited by diamide
the mutant of isoform cyMDH1 shows slightly increased activity compared to the wild type enzyme. The mutant of isoform cyMDH2 shows slightly decreased activity compared to the wild type enzyme
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
construction of enzyme-deficient mutants by pmdh1 and pmdh2 genes disruption by T-DNA insertion, mutant seedlings mobilize their triacylglycerol very slowly and growth are insensitive to 2,4-dichlorophenoxybutyric acid, phenotype, overview
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
construction of knockout single and double mutants, homozygous T-DNA insertion lines for single and double mutations, for the highly expressed mMDH1 and lower expressed mMDH2 isozymes, mmdh1mmdh2 mutant has no detectable mMDH activity but is viable, albeit small and slow growing. Quantitative proteome analysis of mitochondria shows changes in other mitochondrial NAD-linked dehydrogenases, indicating a reorganization of such enzymes in the mitochondrial matrix, phenotypes, overview. Complementation of mmdh1mmdh2 with an mMDH cDNA recovers mMDH activity, suppressed respiratory rate, ameliorated changes to photorespiration, and increases plant growth
recombinant His-Sumo-tagged enzyme from Escherichia coli stain BL21 (DE3) by nickel affinity chromatography, proteolytic cleavage of the His-Sumo tag, ultrafiltration, and gel filtration
Thermal properties of NAD malate dehydrogenase and glutamate oxaloacetate transaminase in two genotypes of Arabidopsis thaliana (Cruciferae) from contrasting environments
Peroxisomal malate dehydrogenase is not essential for photorespiration in Arabidopsis but its absence causes an increase in the stoichiometry of photorespiratory CO2 release
Plastidial NAD-dependent malate dehydrogenase A moonlighting protein involved in early chloroplast development through its interaction with an FtsH12-FtsHi protease complex