EC Number |
General Information |
Reference |
---|
1.1.1.37 | 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 |
740165, 740166 |
1.1.1.37 | more |
the active loop on cMDH closing after sequential binding of NADH binding to the enzyme followed by the substrate |
740166 |
1.1.1.37 | evolution |
Arabidopsis thaliana contains 10 MDHs with only one single copy of MDH gene in the chloroplast, which is a plastidlocalized NAD-dependent MDH |
740198 |
1.1.1.37 | 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 |
740198 |
1.1.1.37 | 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 |
740926 |
1.1.1.37 | 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 |
-, 740926 |
1.1.1.37 | physiological function |
regulation of MDH activity, overview |
-, 740926 |
1.1.1.37 | 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 |
-, 740975 |
1.1.1.37 | 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 |
741200 |
1.1.1.37 | 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 |
741200 |