| Name | malate dehydrogenase |
|---|---|
| Synonyms | ME3; Malate dehydrogenase; NADP ME; Pyruvic malic carboxylase; Malic enzyme 3; Mitochondrial NADP(+) dependent malic enzyme 3; Malic enzyme 3s; Mitochondrial NADP(+) dependent malic enzyme 3s |
| Name | oxamate |
|---|---|
| CAS | hexyl 2-(diethylamino)-2-oxoacetate |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 466765 | Rej R: Measurement of aspartate aminotransferase activity: effects of oxamate. . Clin Chem. 1979 Apr;25(4):555-9. |
0(0,0,0,0) | Details |
| 2160721 | Mazo A, Forner A, Domenech C, Busquets M, Gelpi JL, Cortes A: Comparative analysis of the reduction of by human hepatoma and normal liver extracts. Tumour Biol. 1990;11(3):120-8. Experiments performed with mixtures of both purified enzymes and, conversely, by using oxamate, a specific inhibitor of lactate dehydrogenase, reveal that the deviation in Michaelis-Menten behavior observed is due to the reductase activity of lactate dehydrogenase instead of the presence of a novel malate dehydrogenase isoenzyme. |
33(0,1,1,3) | Details |
| 9446610 | Fushinobu S, Ohta T, Matsuzawa H: Homotropic activation via the subunit interaction and allosteric symmetry revealed on analysis of hybrid enzymes of L-lactate dehydrogenase. J Biol Chem. 1998 Jan 30;273(5):2971-6. Oxamate, a competitive inhibitor of L-lactate dehydrogenase, was used to mimic the substrate-induced activation of the wild-type subunit as "a regulatory subunit." The malate dehydrogenase activity of the mutant subunit as "the catalytic subunit" of the hybrid enzymes was measured, and the activity of the mutant subunit was activated on the addition of oxamate. |
32(0,1,1,2) | Details |
| 1750672 | Dobson GP, Veech RL, Hoeger U, Passonneau JV: Enzymatic determination of total CO2 in freeze-clamped animal tissues and plasma. Anal Biochem. 1991 Jun;195(2):232-7. The assay medium comprised 50 mM 2-amino-2-methyl- pH 9.0 at 25 degrees C, 5 mM (PEP), 0.25 mM 5 mM MgCl2, 5 mM mercaptoethanol, 0.02% bovine serum albumin, 10 mM oxamate, PEP carboxylase (0.5 units/ml), and malate dehydrogenase (0.5 units/ml). |
7(0,0,1,2) | Details |
| 17636950 | Choi SR, Pradhan A, Hammond NL, Chittiboyina AG, Tekwani BL, Avery MA: Design, synthesis, and biological evaluation of Plasmodium falciparum lactate dehydrogenase inhibitors. J Med Chem. 2007 Aug 9;50(16):3841-50. Epub 2007 Jul 18. It is known that the oxamate moiety, a analog, alone shows higher inhibition against pfLDH than human LDHs, suggesting that it can be used for the development of selective inhibitors. They also have micromolar range activities against Plasmodium falciparum malate dehydrogenase (pfMDH), which may fill the role of pfLDH when the activity of pfLDH is reduced. |
1(0,0,0,1) | Details |
| 18922152 | Thornburg JM, Nelson KK, Clem BF, Lane AN, Arumugam S, Simmons A, Eaton JW, Telang S, Chesney J: Targeting aspartate aminotransferase in breast cancer. . Breast Cancer Res. 2008;10(5):R84. Epub 2008 Oct 15. Aspartate aminotransferase (AAT) functions in tandem with malate dehydrogenase to transfer electrons from across the inner mitochondrial membrane. Oxamate is an inhibitor of both LDH and AAT, and we hypothesised that oxamate may disrupt the metabolism and growth of breast adenocarcinoma cells. |
1(0,0,0,1) | Details |