EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.42 | R211M | disruption of the seven-membered inter-domain ionic network. In wild-type enzyme the unfolding and folding transitions occurrs at slightly different denaturant concentrations even after prolonged equilibration time. The difference between the folding and the unfolding profiles is decreased in the mutant R211M | Aeropyrum pernix |
EC Number | General Stability | Organism |
---|---|---|
1.1.1.42 | the inter-domain ionic network might be responsible for additional stabilization through a significant kinetic barrier in the unfolding pathway that can explain the larger difference observed between the folding and unfolding transitions of the wild type comparted to the mutant enzyme R211M | Aeropyrum pernix |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.42 | Aeropyrum pernix | Q9YE81 | - |
- |
1.1.1.42 | Aeropyrum pernix DSM 11879 | Q9YE81 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.42 | isocitrate + NADP+ | - |
Aeropyrum pernix | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.42 | isocitrate + NADP+ | - |
Aeropyrum pernix DSM 11879 | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.42 | dimer | dissociation from dimer to monomer at pH 3.0 | Aeropyrum pernix |
1.1.1.42 | monomer | dissociation from dimer to monomer at pH 3.0 | Aeropyrum pernix |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.42 | 50 | - |
assay at | Aeropyrum pernix |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.42 | 7.5 | - |
assay at | Aeropyrum pernix |