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Literature summary extracted from

  • Takeya, M.; Ito, S.; Sukigara, H.; Osanai, T.
    Purification and characterisation of malate dehydrogenase from Synechocystis sp. PCC 6803 Biochemical barrier of the oxidative tricarboxylic acid cycle (2018), Front. Plant Sci., 9, 947 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.37 fumarate the reductive reaction catalysed by the enzyme is activated by fumarate. Enzyme activity rises approximately 170 and 190% with the addition of 1 and 10 mM fumarate, respectively Synechocystis sp. PCC 6803

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.37 expressed in Escherichia coli BL21 cells Synechocystis sp. PCC 6803

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.37 Cu2+ in the presence of 1 mM Cu2+, the enzyme activity decreases to approximately 40% of normal activity Synechocystis sp. PCC 6803
1.1.1.37 NAD+ substrate inhibition Synechocystis sp. PCC 6803

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.37 0.012
-
 oxaloacetate at pH 6.5 and 50°C Synechocystis sp. PCC 6803
1.1.1.37 0.03
-
 NADH at pH 6.5 and 45°C Synechocystis sp. PCC 6803
1.1.1.37 0.58
-
 NAD+ at pH 8.0 and 45°C Synechocystis sp. PCC 6803
1.1.1.37 2.6
-
 (S)-malate at pH 8.0 and 50°C Synechocystis sp. PCC 6803

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.37 Co2+ the enzyme activity increases approximately 140 % with the addition of 1mM Co2+ Synechocystis sp. PCC 6803
1.1.1.37 Mg2+ the reductive reaction catalysed by the enzyme is activated by magnesium ions. The enzyme activity increases approximately 160 % with the addition of 1mM Mg2+. In the presence of 10 mM MgCl2, the activity of the enzyme increases to approximately 190% Synechocystis sp. PCC 6803
1.1.1.37 additional information enzyme activity cannot be measured in the presence of 10 mM calcium, manganese, cobalt, zinc, or copper ions due to the formation of a precipitate Synechocystis sp. PCC 6803

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+ Synechocystis sp. PCC 6803
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Synechocystis sp. PCC 6803 the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle (S)-malate + NAD+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Synechocystis sp. PCC 6803
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.37 glutathione-Sepharose column chromatography Synechocystis sp. PCC 6803

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.37 (S)-malate + NAD+
-
 Synechocystis sp. PCC 6803 oxaloacetate + NADH + H+
-
 r
1.1.1.37 additional information the enzyme has no activity toward NADP+ and NADPH both in vitro and in vivo Synechocystis sp. PCC 6803 ?
-
-
1.1.1.37 oxaloacetate + NADH + H+ the enzyme is more efficient in the reductive reaction in the tricarboxylic acid cycle Synechocystis sp. PCC 6803 (S)-malate + NAD+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.37 ? x * 50000, SDS-PAGE Synechocystis sp. PCC 6803

Synonyms

EC Number Synonyms Comment Organism
1.1.1.37 MDH
-
 Synechocystis sp. PCC 6803

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.37 45
-
 temperature optimum for the reductive reaction Synechocystis sp. PCC 6803
1.1.1.37 50
-
 temperature optimum for the oxidative reaction Synechocystis sp. PCC 6803

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.37 0.21
-
 NAD+ at pH 8.0 and 45°C Synechocystis sp. PCC 6803
1.1.1.37 0.43
-
 (S)-malate at pH 8.0 and 50°C Synechocystis sp. PCC 6803
1.1.1.37 0.71
-
 oxaloacetate at pH 6.5 and 50°C Synechocystis sp. PCC 6803
1.1.1.37 0.97
-
 NADH at pH 6.5 and 45°C Synechocystis sp. PCC 6803

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.37 6.5
-
 pH optimum for the reductive reaction Synechocystis sp. PCC 6803
1.1.1.37 8
-
 pH optimum for the oxidative reaction Synechocystis sp. PCC 6803

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.37 NAD+
-
 Synechocystis sp. PCC 6803
1.1.1.37 NADH
-
 Synechocystis sp. PCC 6803

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.37 14.5
-
 NAD+ at pH 8.0 and 45°C Synechocystis sp. PCC 6803

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.37 0.165
-
 (S)-malate at pH 8.0 and 50°C Synechocystis sp. PCC 6803
1.1.1.37 0.357
-
 NAD+ at pH 8.0 and 45°C Synechocystis sp. PCC 6803
1.1.1.37 32.3
-
 NADH at pH 6.5 and 45°C Synechocystis sp. PCC 6803
1.1.1.37 59.5
-
 oxaloacetate at pH 6.5 and 50°C Synechocystis sp. PCC 6803