EC Number | Cloned (Comment) | Organism |
---|---|---|
2.6.1.1 | gene aspC, expression of wild-type and K109 mutants in Escherichia coli BL21(DE3) | Thermus thermophilus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.6.1.1 | K109S | site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine, increase in pKa value | Thermus thermophilus |
2.6.1.1 | K109V | site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine | Thermus thermophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.1 | 2-methyl-DL-aspartate | binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex | Thermus thermophilus | |
2.6.1.1 | Maleate | binds noncovalently to the pyridoxal 5'-phosphate form of the enzyme | Thermus thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.1 | additional information | - |
additional information | kinetics | Escherichia coli | |
2.6.1.1 | additional information | - |
additional information | kinetics | Thermus thermophilus | |
2.6.1.1 | additional information | - |
additional information | wild-type and mutants | Escherichia coli | |
2.6.1.1 | additional information | - |
additional information | wild-type and mutants | Thermus thermophilus | |
2.6.1.1 | 1.7 | - |
L-aspartate | wild-type, pH 8.0, 25°C | Thermus thermophilus | |
2.6.1.1 | 2.4 | - |
2-oxoglutarate | wild-type, pH 8.0, 25°C | 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 | Escherichia coli | - |
oxaloacetate + L-glutamate | - |
? | |
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 | Escherichia coli | - |
- |
- |
2.6.1.1 | Thermus thermophilus | Q56232 | - |
- |
2.6.1.1 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q56232 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.6.1.1 | L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate | active site structure, substrate recognition mechanism | Escherichia coli | |
2.6.1.1 | L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate | active site structure, substrate recognition mechanism | Thermus thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.1 | L-alanine + 2-oxoglutarate | - |
Thermus thermophilus | pyruvate + L-glutamate | - |
r | |
2.6.1.1 | L-alanine + 2-oxoglutarate | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | pyruvate + L-glutamate | - |
r | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
? | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Escherichia coli | oxaloacetate + L-glutamate | - |
r | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | - |
Thermus thermophilus | oxaloacetate + L-glutamate | - |
? | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | enzyme can also act on neutral amino acid substrates due to a substrate-binding pocket with a more flexible conformation, Lys109 is the major determinant for the acidic substrate specificity | 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 | enzyme can also act on neutral amino acid substrates due to a substrate-binding pocket with a more flexible conformation, Lys109 is the major determinant for the acidic substrate specificity | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | oxaloacetate + L-glutamate | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.1 | AspAT | - |
Escherichia coli |
2.6.1.1 | AspAT | - |
Thermus thermophilus |
2.6.1.1 | More | aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates | Escherichia coli |
2.6.1.1 | More | aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates | Thermus thermophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.1 | 120 | - |
2-oxoglutarate | wild-type, pH 8.0, 25°C | Thermus thermophilus | |
2.6.1.1 | 120 | - |
L-aspartate | wild-type, pH 8.0, 25°C | Thermus thermophilus |