Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Haloarcula marismortui |
Crystallization (Comment) | Organism |
---|---|
sitting drop reverse vapour diffusion method, crystal structure of the R207S/R292S mutant of malate dehydrogenase is solved at 1.95 A | Haloarcula marismortui |
Protein Variants | Comment | Organism |
---|---|---|
R207S/R292S | the numbering is not equivalent to the numbering of UniProt. The mutations, located at the dimer-dimer interface, disrupt two inter-dimeric salt bridge clusters that are essential for wild-type tetramer stabilisation. Association of active dimers into tetramers is weakened | Haloarcula marismortui |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloarcula marismortui | Q07841 | - |
- |
Haloarcula marismortui DSM 3752 | Q07841 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Haloarcula marismortui |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
oxaloacetate + NADH + H+ | - |
Haloarcula marismortui | (S)-malate + NAD+ | - |
? | |
oxaloacetate + NADH + H+ | - |
Haloarcula marismortui DSM 3752 | (S)-malate + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | wild-type enzyme and R207S/R292S mutant enzyme can both exist as dimeric species depending on solvent conditions. F- and SO42-, as well as the NADH cofactor, stabilize the dimeric form of the wild-type protein | Haloarcula marismortui |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Haloarcula marismortui |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Haloarcula marismortui |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Haloarcula marismortui |