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evolution
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the plasma membrane-associated isozyme belongs belongs to the lactate dehydrogenase/MDH superfamily, MDH type 2 family
evolution
the three different enzyme forms in cytosol, peroxisome and mitochondrion are encoded by three different genes in Saccharomyces cerevisiae, but by only two genes in Yarrowia lipolytica, where the second gene is differentiated into cytosolic and peroxisomal isozymes by alternative splicing, overview
evolution
Arabidopsis thaliana contains 10 MDHs with only one single copy of MDH gene in the chloroplast, which is a plastidlocalized NAD-dependent MDH
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus. The other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
the enzyme belongs to the MalDH/LDH superfamily, which is divided into several phylogenetically related groups, lactate dehydrogenases (LDHs) and malate dehydrogenases (MalDHs) belong to a wide group of 2-oxoacid:NAD(P)-dependent dehydrogenases that catalyze the reversible conversion of 2-hydroxyacids to the corresponding 2-oxoacids, evolutionary history of the LDHs and MalDHs, overview. The enzyme structure belongs to the NAD(P)-binding Rossmann-like domain CATH superfamily
evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
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evolution
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the plasma membrane-associated isozyme belongs belongs to the lactate dehydrogenase/MDH superfamily, MDH type 2 family
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evolution
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the enzyme belongs to the MalDH/LDH superfamily, which is divided into several phylogenetically related groups, lactate dehydrogenases (LDHs) and malate dehydrogenases (MalDHs) belong to a wide group of 2-oxoacid:NAD(P)-dependent dehydrogenases that catalyze the reversible conversion of 2-hydroxyacids to the corresponding 2-oxoacids, evolutionary history of the LDHs and MalDHs, overview. The enzyme structure belongs to the NAD(P)-binding Rossmann-like domain CATH superfamily
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evolution
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MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
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malfunction
absence of either the peroxisomal or the cytosolic form of the MDH does not affect growth rate, irrespective of the carbon source
malfunction
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exposure of maize plants to excess concentrations of Zn2+ and Cu2+ in the hydroponic solution inhibited lateral root growth, decreased malate dehydrogenase activity and changed isoform profiles
malfunction
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knockdown of MDH1 in young human dermal fibroblasts and the IMR90 human fibroblast cell line results in the appearance of significant cellular senescence features, including senescence-associated beta-galactosidase staining, flattened and enlarged morphology, increased population doubling time, and elevated p16INK4A and p21CIP1 protein levels. The NAD/NADH ratio is decreased by 90% in MDH1 knockdown dermal fibroblasts but only by about 30% in MDH2 knockdown dermal fibroblasts
malfunction
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
malfunction
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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
malfunction
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Arabidopsis mutants lacking the enzyme are embryo-lethal, and constitutive silencing causes a pale, dwarfed phenotype
malfunction
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in a flo16 knockout mutant, the transition from sucrose to starch is partially disrupted during mutant grain filling
malfunction
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
malfunction
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in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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malfunction
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in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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malfunction
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in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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malfunction
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in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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malfunction
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in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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malfunction
-
exposure of maize plants to excess concentrations of Zn2+ and Cu2+ in the hydroponic solution inhibited lateral root growth, decreased malate dehydrogenase activity and changed isoform profiles
-
malfunction
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in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
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metabolism
malate dehydrogenase utilizes NAD/NADH as coenzyme to reversibly catalyze the oxidation/reduction of the malate/oxaloacetate. The mitochondrial isoenzyme (mMDH) catalyzes the oxidation of malate, and is the last step of the citric acid cycle, while the cytoplasmic isoenzyme (cMDH) primarily reduces oxaloacetate in the cytoplasm
metabolism
malate dehydrogenase utilizes NAD/NADH as coenzyme to reversibly catalyze the oxidation/reduction of the malate/oxaloacetate. The mitochondrial isoenzyme (mMDH) catalyzes the oxidation of malate, and is the last step of the citric acid cycle, while the cytoplasmic isoenzyme (cMDH) primarily reduces oxaloacetate in the cytoplasm
metabolism
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the enzyme is involved in the Krebs cycle (catabolism), glyoxylate and Hatch-Slack cycles, and malate metabolism, as well as other anabolic processes
metabolism
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the enzyme plays crucial roles in many metabolic pathways, including the tricarboxylic acid (TCA) cycle, energy generation and the formation of metabolites for biosynthesis
metabolism
the enzyme plays crucial roles in many metabolic pathways, including the tricarboxylic acid (TCA) cycle, energy generation and the formation of metabolites for biosynthesis
metabolism
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isoform MDH1 generates malate with carbons derived from glutamine, thus enabling utilization of glucose carbons for glycolysis and for biomass
metabolism
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isoform MDH3 is an essential component of the gluconeogenesis pathway that generates glucose from noncarbohydrate carbon substrates and is involved in the reoxidation of NADH produced by fatty-acid beta-oxidation in glyoxysomes
metabolism
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the enzyme gene FLO16 plays a critical role in redox homeostasis that is important for compound starch grain formation and subsequent starch biosynthesis in rice endosperm
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle
metabolism
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
metabolism
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
metabolism
when the competent catalytic state is reached, LDH catalyzes the direct transfer of a hydride ion from the pro-R face of NADH to the C2 carbon of pyruvate to produce lactate, whereas MalDH transforms oxaloacetate into malate
metabolism
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the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
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metabolism
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the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
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metabolism
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when the competent catalytic state is reached, LDH catalyzes the direct transfer of a hydride ion from the pro-R face of NADH to the C2 carbon of pyruvate to produce lactate, whereas MalDH transforms oxaloacetate into malate
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
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metabolism
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the enzyme plays crucial roles in many metabolic pathways, including the tricarboxylic acid (TCA) cycle, energy generation and the formation of metabolites for biosynthesis
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metabolism
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the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
-
metabolism
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in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
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physiological function
cyMDH is an enzyme crucial for malate synthesis in the cytosol. Involvement of MdcyMDH directly in malate synthesis and indirectly in malate accumulation through the regulation of genes/enzymes associated with malate degradation and transportation, gluconeogenesis and the tricarboxylic acid cycle.
physiological function
cyMDH is an enzyme crucial for malic acid synthesis in the cytosol. Role of the apple cyMDH gene in growth and tolerance to cold and salt stresses. cyMDH was sensitive to cold and salt stresses. cyMDH overexpression favourably contributes to cell and plant growth and confers stress tolerance in the apple
physiological function
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MDH is an essential enzyme in the tricarboxylic acid cycle. Inhibition of mMDH activity affects cell energy production, probably leading to the inhibition of proliferation. Inhibition of mMDH activity by DIF-1 and 2-MIDIF-1 can be one of the mechanisms to induce anti-proliferative effects, independent of the inhibition of the Wnt/beta-catenin signaling pathway
physiological function
mitochondrial and cytosolic MDH isozymes are required for maintaining the balance of NAD+ and NADH in mitochondria and cytosol
physiological function
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
physiological function
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
physiological function
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besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
physiological function
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besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
physiological function
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besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
physiological function
cytosolic NAD-dependent malate dehydrogenase is an enzyme crucial for malate synthesis in the cytosol
physiological function
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MDH1 plays a critical role in the cellular senescence of human fibroblasts. MDH1 is the major regulator of the cofactor NAD, the loss of which induces cellular senescence
physiological function
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
physiological function
MDH is an energy-supplying enzyme, that catalyzes the interconversion of malate and oxaloacetate and plays crucial roles in several metabolic pathways including the citric acid cycle. The phosphorylation of enzyme MDH by serine/threonine protein kinases negatively regulates its activity
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
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regulation of MDH activity, overview
physiological function
the mitochondrial isozyme is allosterically regulated by citrate
physiological function
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
physiological function
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plastidial NAD-dependent malate dehydrogenase 1 negatively regulates salt stress response by reducing the vitamin B6 content. The enzyme negatively regulates salt stress-induced pyridoxine accumulation. Enzyme-overexpressing plants exhibit salt stress-sensitive phenotypes
physiological function
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the enzyme has strong effects on starch biosynthesis during seed development
physiological function
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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
physiological function
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the enzyme is essential for early etioplast and chloroplast development due to its moonlighting role in stabilizing FtsH12, distinct from its enzymatic function
physiological function
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the enzyme isoform MDH1 plays a critical role in replenishing cytosolic NAD+ to support increased glycolysis during proliferation
physiological function
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
physiological function
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the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
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physiological function
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the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
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physiological function
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regulation of MDH activity, overview
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physiological function
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mitochondrial and cytosolic MDH isozymes are required for maintaining the balance of NAD+ and NADH in mitochondria and cytosol
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physiological function
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besides its function in malate synthesis, MDH is responsible for the exchange of reducing equivalents between metabolic pathways in distinct cell compartments
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physiological function
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the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
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physiological function
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MDH is an energy-supplying enzyme, that catalyzes the interconversion of malate and oxaloacetate and plays crucial roles in several metabolic pathways including the citric acid cycle. The phosphorylation of enzyme MDH by serine/threonine protein kinases negatively regulates its activity
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physiological function
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the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
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physiological function
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regulation of MDH activity, overview
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physiological function
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the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
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physiological function
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the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
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additional information
inverse correlation between mMDH and ascorbate content
additional information
inverse correlation between mMDH and ascorbate content
additional information
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mMDH inhibition is of minor relevance for the growth inhibition caused by paullones
additional information
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a significant decrease of both mass and elongation of maize roots and shoots, as well as loss of root turgor and completely repressed lateral root growth were demonstrated in 0.1 mM Cu2+ and 5 mM Zn2+ treatments, overview
additional information
possible role for alternative splicing in the regulation of MDH compartmentalization in this yeast, gene YlMDH2 encodes the cytosolic and peroxisomal forms of MDH
additional information
possible role for alternative splicing in the regulation of MDH compartmentalization in this yeast, gene YlMDH2 encodes the cytosolic and peroxisomal forms of MDH
additional information
molecular dynamics simulation at higher temperatures were used to reconstruct structures from the crystal structure of TtMDH. At the simulated structure of 80°C, a large change occurs around the active site such that with increasing temperature, a mobile loop is closed to co-substrate binding region. The thermal-induced conformational change of the co-substrate binding loop of TtMDH may contribute to the essential movement of the enzyme for admitting NAD and may benefit the enzyme's activity
additional information
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molecular dynamics simulation at higher temperatures were used to reconstruct structures from the crystal structure of TtMDH. At the simulated structure of 80°C, a large change occurs around the active site such that with increasing temperature, a mobile loop is closed to co-substrate binding region. The thermal-induced conformational change of the co-substrate binding loop of TtMDH may contribute to the essential movement of the enzyme for admitting NAD and may benefit the enzyme's activity
additional information
the active loop on cMDH closing after sequential binding of NADH binding to the enzyme followed by the substrate
additional information
MalDH is an enzyme with intermediate properties between allosteric LDHs and non-allosteric tetrameric MalDHs. The catalytic residue is histidine H195. The structure of Ignicoccus islandicus MalDH resembles that of canonical LDHs. The amino acid at position 102 is considered as the most important substrate-discriminating residue between LDHs and MalDHs. Structure-function analysis and comparisons, overview
additional information
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MalDH is an enzyme with intermediate properties between allosteric LDHs and non-allosteric tetrameric MalDHs. The catalytic residue is histidine H195. The structure of Ignicoccus islandicus MalDH resembles that of canonical LDHs. The amino acid at position 102 is considered as the most important substrate-discriminating residue between LDHs and MalDHs. Structure-function analysis and comparisons, overview
additional information
sequence-similarity networks analysis
additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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MalDH is an enzyme with intermediate properties between allosteric LDHs and non-allosteric tetrameric MalDHs. The catalytic residue is histidine H195. The structure of Ignicoccus islandicus MalDH resembles that of canonical LDHs. The amino acid at position 102 is considered as the most important substrate-discriminating residue between LDHs and MalDHs. Structure-function analysis and comparisons, overview
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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sequence-similarity networks analysis
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additional information
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a significant decrease of both mass and elongation of maize roots and shoots, as well as loss of root turgor and completely repressed lateral root growth were demonstrated in 0.1 mM Cu2+ and 5 mM Zn2+ treatments, overview
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