EC Number   |
General Information |
Reference |
|---|
    1.1.1.82 | 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 |
| 1.1.1.82 | 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) |
740926 |
| 1.1.1.82 | 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 |
| 1.1.1.82 | malfunction |
Arabidopsis thaliana mutants lacking the NADP-malate dehydrogenase lose the reversible inactivation of catalase activity and the increase in H2O2 levels when exposed to high light. The mutants are slightly affected in growth and accumulate higher levels of NADPH in the chloroplast than the wild-type. Catalase activity and H2O2 levels under high light stress in Arabidopsis thaliana knockout mutants deficient for chloroplastic NADP-MDH, overview |
-, 739249 |
| 1.1.1.82 | metabolism |
the enzyme is involved in the signalling by a H2O2 pulse in high light-stressed plants, overview The malate valve plays a crucial role in transmitting the redox state of the chloroplast to other cell compartments |
-, 739249 |
| 1.1.1.82 | 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 to reduce oxaloacetate to malate, thus regenerating the electron acceptor NADP+. Since NADP-MDH is a strictly redox-regulated, light-activated enzyme that is inactive in the dark, the malate-oxaloacetate shuttle is in the dark or in nonphotosynthetic tissues proposed to be mediated by the constitutively active plastidial NAD-specific MDH isoform (pdNAD-MDH, EC 1.1.1.37), which is is active under both light and dark conditions. 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. NADP-MDH is not crucial for providing electron acceptors in chloroplasts |
741200 |
| 1.1.1.82 | physiological function |
maize enzyme-overexpressing Arabidopsis thaliana plants are tolerant to salt stress (150 mM NaCl) |
762354 |
| 1.1.1.82 | physiological function |
regulation of MDH activity, overview |
-, 740926 |
| 1.1.1.82 | physiological function |
the malate valve plays an essential role in the regulation of catalase activity and the accumulation of a H2O2 signal by transmitting the redox state of the chloroplast to other cell compartments |
-, 739249 |
| 1.1.1.82 | physiological function |
thiol-switch redox regulation of enzyme activity is crucial for maintaining NADPH homeostasis in chloroplasts and plays a crucial role in the optimal growth of plants under short-day or fluctuating light conditions |
762295 |
