EC Number | Cloned (Comment) | Organism |
---|---|---|
2.6.1.1 | cloning, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli AB1157 | Thermus thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.1 | additional information | - |
additional information | kinetics | Thermus thermophilus | |
2.6.1.1 | additional information | - |
additional information | recombinant enzyme | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.1 | L-aspartate + 2-oxoglutarate | Thermus thermophilus | - |
oxaloacetate + L-glutamate | - |
? | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
oxaloacetate + L-glutamate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.6.1.1 | Thermus thermophilus | - |
- |
- |
2.6.1.1 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.6.1.1 | recombinant from overproducing Escherichia coli AB1157 cells, 66fold | Thermus thermophilus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.6.1.1 | L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate | bi bi ping pong reaction kinetic | Thermus thermophilus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 112.1 | - |
purified recombinant enzyme | Thermus thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Thermus thermophilus | oxaloacetate + L-glutamate | - |
? | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Thermus thermophilus | oxaloacetate + L-glutamate | - |
r | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | oxaloacetate + L-glutamate | - |
? | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | oxaloacetate + L-glutamate | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.1 | AspAT | - |
Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 25 | - |
assay at | Thermus thermophilus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | additional information | - |
high thermostability, extra prolyl residues, located at the surface of the protein, are involved | Thermus thermophilus |
2.6.1.1 | additional information | - |
thermal denaturation is irreversible | Thermus thermophilus |
2.6.1.1 | 75 | - |
stable up to | Thermus thermophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 8 | - |
assay at | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.1 | pyridoxal 5'-phosphate | a pyridoxal 5'-phosphate protein | Thermus thermophilus | |
2.6.1.1 | pyridoxal 5'-phosphate | enzyme-bound | Thermus thermophilus |