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Literature summary for 1.1.1.37 extracted from
- Determination of the catalytic mechanism for mitochondrial malate dehydrogenase (2015), Biophys. J., 108, 408-419.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-Thenoyltrifluoroacetone | - |
Homo sapiens |  |
| ADP | - |
Homo sapiens | |
| AMP | - |
Homo sapiens | |
| aspartate | - |
Homo sapiens | |
| ATP | - |
Homo sapiens | |
| citrate | - |
Homo sapiens | |
| fumarate | - |
Homo sapiens | |
| oxaloacetate | at high concentrations | Homo sapiens | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | pH-dependent kinetic mechanism for mMDH, and kinetic modelling for mMDH-catalyzed oxidation of L-malate, detailed overview | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Homo sapiens | 5739 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
about | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NAD+ | Homo sapiens | - |
oxaloacetate + NADH + H+ | - |
r | |
| oxaloacetate + NADH + H+ | Homo sapiens | - |
(S)-malate + NAD+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P40926 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| (S)-malate + NAD+ = oxaloacetate + NADH + H+ | an ordered bi-bi mechanism with coenzyme binding first followed by the binding of substrate is able to explain the kinetic data. The proposed mechanism is similar to, but not identical to, the mechanism determined for the cytoplasmic isoform, cMDH | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NAD+ | - |
Homo sapiens | oxaloacetate + NADH + H+ | - |
r | |
| oxaloacetate + NADH + H+ | - |
Homo sapiens | (S)-malate + NAD+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | the dimer form dissociates to monomer at low enzyme concentration, and at low pH, and is active only in dimer form | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MDH2 | - |
Homo sapiens |
| mitochondrial malate dehydrogenase | - |
Homo sapiens |
| mMDH | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
NAD+ reduction | Homo sapiens |
| 9 | - |
NADH oxidation | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Homo sapiens | |
| NADH | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Homo sapiens |
| physiological function | the mitochondrial isozyme is allosterically regulated by citrate | Homo sapiens |
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