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Literature summary for 1.1.1.37 extracted from
- Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortui (2007), Biochimie, 89, 981-987.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Haloarcula marismortui |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K205A | site-directed mutagenesis, the oligomeric state of the mutant changes with the nature of the anion bound, the mutant is dimeric or tetrameric, overview | Haloarcula marismortui |
| R207S/R292S | site-directed mutagenesis, the oligomeric state of the mutant changes with the nature of the anion bound, the mutant is dimeric or tetrameric, overview | Haloarcula marismortui |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Haloarcula marismortui | |
| 0.012 | - |
NADH | pH 8.0, 25°C, recombinant wild-type enzyme and mutant K205A | Haloarcula marismortui |  |
| 0.13 | - |
oxaloacetate | pH 8.0, 25°C, recombinant wild-type enzyme and mutant K205A | Haloarcula marismortui | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| chloride | binding site structure analysis, structural adaptation in the halophilic protein, residue Lys205 is involved, the anion influences the oligomeric state of the enzyme, overview | Haloarcula marismortui | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NAD+ | Haloarcula marismortui | - |
oxaloacetate + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloarcula marismortui | Q07841 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by gel filtration, hydrophobic interaction chromatography using 4 M KF and 1.3 M ammonium sulfate for elution, followed by dialysis | Haloarcula marismortui |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NAD+ | - |
Haloarcula marismortui | oxaloacetate + NADH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Haloarcula marismortui |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| halophilic malate dehydrogenase | - |
Haloarcula marismortui |
| MalDH | - |
Haloarcula marismortui |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at, reduction reaction | Haloarcula marismortui |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at, reduction reaction | Haloarcula marismortui |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Haloarcula marismortui | |
| NADH | - |
Haloarcula marismortui | |
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Release 2023.1 (January 2023)
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