EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.1.2 | expression in Escherichia coli | Methanocaldococcus jannaschii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.3.2 | Escherichia coli | - |
- |
- |
2.1.3.2 | Methanocaldococcus jannaschii | - |
- |
- |
6.3.1.2 | Methanocaldococcus jannaschii | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.1.2 | recombinant enzyme | Methanocaldococcus jannaschii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoyl phosphate + L-aspartate | - |
Escherichia coli | phosphate + N-carbamoyl-L-aspartate | - |
? | |
2.1.3.2 | carbamoyl phosphate + L-aspartate | - |
Methanocaldococcus jannaschii | phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.3.2 | trimer | - |
Methanocaldococcus jannaschii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.3.2 | aspartate transcarbamoylase | - |
Escherichia coli |
2.1.3.2 | aspartate transcarbamoylase | - |
Methanocaldococcus jannaschii |
2.1.3.2 | ATCase | - |
Escherichia coli |
2.1.3.2 | ATCase | - |
Methanocaldococcus jannaschii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.3.2 | 37 | - |
assay at | Escherichia coli |
2.1.3.2 | 55 | - |
assay at | Methanocaldococcus jannaschii |
6.3.1.2 | 55 | - |
- |
Methanocaldococcus jannaschii |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.1.2 | 40 | 70 | about 50% of maximal activity at 40°C and at 70°C | Methanocaldococcus jannaschii |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.3.2 | 55 | 65 | 4 min, loss of 70% of secondary structure in absence of solutes, Tm is highly enhanced in presence of KCl, NaCl, or alpha and beta isomers of K+-glutamate, NaCl, KCl, glycine, and betaine are not thermoprotective, but trehalose, sucrose, and K+-glutamate are, K+-glutamate raises Tm and maintains enzyme activity, overview | Escherichia coli |
2.1.3.2 | 95 | - |
30 min, stable in solutes, but large loss of secondary structure in absence of solutes, the loss is enhanced in presence of KCl, NaCl, or K+-glutamate, glycine and sucrose are thermoprotective | Methanocaldococcus jannaschii |
2.1.3.2 | 100 | - |
30 min, stable in solutes, but loss of 41% of secondary structure in absence of solutes, the loss is enhanced in presence of KCl, NaCl, or K+-glutamate, glycine and sucrose are thermoprotective | Methanocaldococcus jannaschii |
6.3.1.2 | 57 | - |
midpoint temperature of pure enzyme, none of the small molecules tested significantly stabilizes the enzyme. Stabilization by Escherichia coli GroEL or ribosomal protein L2. Protein-protein interactions appear to be the dominant factor in stabilizing the archael enzyme at the growth temperature (85°C) | Methanocaldococcus jannaschii |