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Literature summary extracted from

  • Dasika, S.K.; Vinnakota, K.C.; Beard, D.A.
    Determination of the catalytic mechanism for mitochondrial malate dehydrogenase (2015), Biophys. J., 108, 408-419.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.37 2-Thenoyltrifluoroacetone
-
 Homo sapiens
1.1.1.37 ADP
-
 Homo sapiens
1.1.1.37 AMP
-
 Homo sapiens
1.1.1.37 aspartate
-
 Homo sapiens
1.1.1.37 ATP
-
 Homo sapiens
1.1.1.37 citrate
-
 Homo sapiens
1.1.1.37 fumarate
-
 Homo sapiens
1.1.1.37 oxaloacetate at high concentrations Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.37 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.37 mitochondrion
-
 Homo sapiens 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.37 70000
-
 about Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.37 (S)-malate + NAD+ Homo sapiens
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Homo sapiens
-
 (S)-malate + NAD+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Homo sapiens P40926
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.37 (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
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.37 heart
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.37 (S)-malate + NAD+
-
 Homo sapiens oxaloacetate + NADH + H+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Homo sapiens (S)-malate + NAD+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.37 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

EC Number Synonyms Comment Organism
1.1.1.37 MDH2
-
 Homo sapiens
1.1.1.37 mitochondrial malate dehydrogenase
-
 Homo sapiens
1.1.1.37 mMDH
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.37 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.37 6.5
-
 NAD+ reduction Homo sapiens
1.1.1.37 9
-
 NADH oxidation Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.37 NAD+
-
 Homo sapiens
1.1.1.37 NADH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.1.1.37 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
1.1.1.37 physiological function the mitochondrial isozyme is allosterically regulated by citrate Homo sapiens