EC Number |
General Information |
Reference |
---|
1.1.1.37 | metabolism |
the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle |
761237, 761615, 761624 |
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 | 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) |
-, 761123 |
1.1.1.37 | 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 |
-, 761765 |
1.1.1.37 | more |
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 |
-, 723482 |
1.1.1.37 | more |
inverse correlation between mMDH and ascorbate content |
713318 |
1.1.1.37 | more |
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 |
-, 761765 |
1.1.1.37 | more |
mMDH inhibition is of minor relevance for the growth inhibition caused by paullones |
711909 |
1.1.1.37 | more |
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 |
741286 |
1.1.1.37 | more |
possible role for alternative splicing in the regulation of MDH compartmentalization in this yeast, gene YlMDH2 encodes the cytosolic and peroxisomal forms of MDH |
721236 |