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Literature summary for 1.1.1.37 extracted from
- 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 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 cells | Synechocystis sp. PCC 6803 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | in the presence of 1 mM Cu2+, the enzyme activity decreases to approximately 40% of normal activity | Synechocystis sp. PCC 6803 | |
| NAD+ | substrate inhibition | Synechocystis sp. PCC 6803 | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.012 | - |
oxaloacetate | at pH 6.5 and 50°C | Synechocystis sp. PCC 6803 | |
| 0.03 | - |
NADH | at pH 6.5 and 45°C | Synechocystis sp. PCC 6803 | |
| 0.58 | - |
NAD+ | at pH 8.0 and 45°C | Synechocystis sp. PCC 6803 | |
| 2.6 | - |
(S)-malate | at pH 8.0 and 50°C | Synechocystis sp. PCC 6803 | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | the enzyme activity increases approximately 140 % with the addition of 1mM Co2+ | Synechocystis sp. PCC 6803 | |
| 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 | |
| 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)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NAD+ | Synechocystis sp. PCC 6803 | - |
oxaloacetate + NADH + H+ | - |
r | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Synechocystis sp. PCC 6803 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| glutathione-Sepharose column chromatography | Synechocystis sp. PCC 6803 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NAD+ | - |
Synechocystis sp. PCC 6803 | oxaloacetate + NADH + H+ | - |
r | |
| additional information | the enzyme has no activity toward NADP+ and NADPH both in vitro and in vivo | Synechocystis sp. PCC 6803 | ? | - |
- |
|
| 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
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 50000, SDS-PAGE | Synechocystis sp. PCC 6803 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MDH | - |
Synechocystis sp. PCC 6803 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
temperature optimum for the reductive reaction | Synechocystis sp. PCC 6803 |
| 50 | - |
temperature optimum for the oxidative reaction | Synechocystis sp. PCC 6803 |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.21 | - |
NAD+ | at pH 8.0 and 45°C | Synechocystis sp. PCC 6803 | |
| 0.43 | - |
(S)-malate | at pH 8.0 and 50°C | Synechocystis sp. PCC 6803 | |
| 0.71 | - |
oxaloacetate | at pH 6.5 and 50°C | Synechocystis sp. PCC 6803 | |
| 0.97 | - |
NADH | at pH 6.5 and 45°C | Synechocystis sp. PCC 6803 | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
pH optimum for the reductive reaction | Synechocystis sp. PCC 6803 |
| 8 | - |
pH optimum for the oxidative reaction | Synechocystis sp. PCC 6803 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Synechocystis sp. PCC 6803 | |
| NADH | - |
Synechocystis sp. PCC 6803 | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 14.5 | - |
NAD+ | at pH 8.0 and 45°C | Synechocystis sp. PCC 6803 | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.165 | - |
(S)-malate | at pH 8.0 and 50°C | Synechocystis sp. PCC 6803 | |
| 0.357 | - |
NAD+ | at pH 8.0 and 45°C | Synechocystis sp. PCC 6803 | |
| 32.3 | - |
NADH | at pH 6.5 and 45°C | Synechocystis sp. PCC 6803 | |
| 59.5 | - |
oxaloacetate | at pH 6.5 and 50°C | Synechocystis sp. PCC 6803 | |
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