EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.6.1.1 | the X-ray structure of the PfAspAT homodimer at a resolution of 2.8 A is reported. While the overall fold is similar to the currently available structures of other AspATs, the structure presented shows a significant divergence in the conformation of the N-terminal residues | Plasmodium falciparum |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.6.1.1 | DELTA1-13 | truncation of these noncatalytic residues reduces enzyme activity and a peptide containing these amino acids inhibits PfAspAT in vitro and in the lysate of cultured parasites | Plasmodium falciparum |
2.6.1.1 | DELTA1-7 | truncation of the first seven amino acids only minorly reduces enzymatic activity | Plasmodium falciparum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.1 | hydroxylamine | inhibition of PfAspAT abolishes all glutamate oxaloacetate transamination activity in the cytoplasm of cultured parasites, demonstrating that no other enzyme within the cytoplasm can complement PfAspAT activity | Plasmodium falciparum |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.6.1.1 | cytoplasm | - |
Plasmodium falciparum | 5737 | - |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.6.1.1 | Plasmodium falciparum | O96142 | - |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 0.14 | - |
substrates: L-asparagine + 2-oxoglutarate, pH 8, 37°C | Plasmodium falciparum |
2.6.1.1 | 0.16 | - |
substrates: L-tryptophan + 2-oxoglutarate, pH 8, 37°C | Plasmodium falciparum |
2.6.1.1 | 0.24 | - |
substrates: L-tyrosine + 2-oxoglutarate, pH 8, 37°C | Plasmodium falciparum |
2.6.1.1 | 0.28 | - |
substrates: L-phenylalanine + 2-oxoglutarate, pH 8, 37°C | Plasmodium falciparum |
2.6.1.1 | 2.67 | - |
substrates: L-aspartate + 2-oxoglutarate, pH 8, 37°C | Plasmodium falciparum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.1 | L-asparagine + 2-oxoglutarate | specific activity: 0.14 micromol/min/mg | Plasmodium falciparum | 4-amino-2,4-dioxobutanoate + L-glutamate | - |
? | |
2.6.1.1 | L-aspartate + 2-oxoglutarate | specific activity: 2.67 micromol/min/mg | Plasmodium falciparum | oxaloacetate + L-glutamate | - |
? | |
2.6.1.1 | L-phenylalanine + 2-oxoglutarate | specific activity: 0.28 micromol/min/mg | Plasmodium falciparum | 2-oxo-3-phenylpropanoate + L-glutamate | - |
? | |
2.6.1.1 | L-tryptophan + 2-oxoglutarate | specific activity: 0.16 micromol/min/mg | Plasmodium falciparum | 3-(1H-indol-3-yl)-2-oxopropanoate + L-glutamate | - |
? | |
2.6.1.1 | L-tyrosine + 2-oxoglutarate | specific activity: 0.24 micromol/min/mg | Plasmodium falciparum | 3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.6.1.1 | homodimer | - |
Plasmodium falciparum |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.1 | AspAT | - |
Plasmodium falciparum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 37 | - |
assay at | Plasmodium falciparum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.6.1.1 | 8 | - |
assay at | Plasmodium falciparum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.1 | pyridoxal 5'-phosphate | - |
Plasmodium falciparum |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.6.1.1 | 0.069 | - |
pH 8, 37°C | Plasmodium falciparum | hydroxylamine |