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Literature summary for 1.1.1.37 extracted from

  • Dasika, S.K.; Vinnakota, K.C.; Beard, D.A.
    Characterization of the kinetics of cardiac cytosolic malate dehydrogenase and comparative analysis of cytosolic and mitochondrial isoforms (2015), Biophys. J., 108, 420-430.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information pH-dependent kinetic mechanism for cMDH, and kinetic modelling for cMDH-catalyzed oxidation of L-malate, detailed overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

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 P40925
-
-

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 mitochondrial isoform, mMDH 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

Synonyms

Synonyms Comment Organism
cMDH
-
Homo sapiens
cytosolic malate dehydrogenase
-
Homo sapiens
Mdh1
-
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
additional information the active loop on cMDH closing after sequential binding of NADH binding to the enzyme followed by the substrate Homo sapiens