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	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	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	-, 761765	
1.1.1.37	evolution	the plasma membrane-associated isozyme belongs belongs to the lactate dehydrogenase/MDH superfamily, MDH type 2 family	-, 723059	
1.1.1.37	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	721236	
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	malfunction	absence of either the peroxisomal or the cytosolic form of the MDH does not affect growth rate, irrespective of the carbon source	721236	
1.1.1.37	malfunction	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	762123	
1.1.1.37	malfunction	Arabidopsis mutants lacking the enzyme are embryo-lethal, and constitutive silencing causes a pale, dwarfed phenotype	762124