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Literature summary extracted from

  • Genda, T.; Nakamatsu, T.; Ozaki, H.
    Purification and characterization of malate dehydrogenase from Corynebacterium glutamicum (2003), J. Biosci. Bioeng., 95, 562-566.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.37 citrate oxidation of malate to oxaloacetate Corynebacterium glutamicum
1.1.1.37 isocitrate oxidation of malate to oxaloacetate Corynebacterium glutamicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.37 (NH4)2SO4 reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate Corynebacterium glutamicum
1.1.1.37 2-oxoglutarate reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate Corynebacterium glutamicum
1.1.1.37 citrate reduction of oxaloacetate to malate Corynebacterium glutamicum
1.1.1.37 isocitrate reduction of oxaloacetate to malate Corynebacterium glutamicum
1.1.1.37 succinate slight inhibition of reduction of oxaloacetate Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.37 0.025
-
 oxaloacetate pH 6.5, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.041
-
 NADH pH 8.0, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.057
-
 oxaloacetate pH 8.0, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.07
-
 NADH pH 6.5, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.1
-
 NADH pH 9.5, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.2
-
 oxaloacetate pH 9.5, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.25
-
 NADPH pH 6.5, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.4
-
 NAD+ pH 10.5, 20-23°C Corynebacterium glutamicum
1.1.1.37 0.55
-
 oxaloacetate pH 6.5, 20.23°C Corynebacterium glutamicum
1.1.1.37 0.8
-
 L-malate pH 10.5, 20-23°C Corynebacterium glutamicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.37 33000
-
 4 * 33000, SDS-PAGE Corynebacterium glutamicum
1.1.1.37 130000
-
 gel filtration Corynebacterium glutamicum

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Corynebacterium glutamicum Q8NN33 ATCC 14067
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.37
-
 Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.37 517
-
-
 Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.37 (S)-malate + NAD+
-
 Corynebacterium glutamicum oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NADP+
-
 Corynebacterium glutamicum oxaloacetate + NADPH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.37 tetramer 4 * 33000, SDS-PAGE Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.37 6.5
-
 reduction of oxaloacetate to L-malate with NADH as coenzyme, at oxaloacetate concentration of 0.05 mM. Reduction of oxalacetate to L-malate with NADPH as coenzyme Corynebacterium glutamicum
1.1.1.37 8
-
 reduction of oxaloacetate to L-malate with NADH as coenzyme, at oxaloacetate concentration of 0.1 mM Corynebacterium glutamicum
1.1.1.37 9
-
 around, activity is to low to depict a pH curve Corynebacterium glutamicum
1.1.1.37 9.5
-
 reduction of oxaloacetate to L-malate with NADH as coenzyme, at oxaloacetate concentration of 1.0 mM Corynebacterium glutamicum
1.1.1.37 10.5
-
 oxidation of L-malate to oxalacetete with NAD+ as coenzyme Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.37 NAD+
-
 Corynebacterium glutamicum
1.1.1.37 NADH almost equally active both for NADH and NADPH on the bases of the turnover number values at pH 6.5, which is optimal for both coenzymes Corynebacterium glutamicum
1.1.1.37 NADP+
-
 Corynebacterium glutamicum
1.1.1.37 NADPH almost equally active both for NADH and NADPH on the bases of the turnover number values at pH 6.5, which is optimal for both coenzymes Corynebacterium glutamicum