EC Number   |
Title |
Organism |
|---|
    2.1.3.2 | Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima Fused catalytic and regulatory polypeptides form an allosteric enzyme |
Thermotoga maritima |
| 2.1.3.2 | Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima Fused catalytic and regulatory polypeptides form an allosteric enzyme |
Thermotoga maritima DSM 3109 |
| 2.1.3.2 | Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes |
Escherichia coli |
| 2.1.3.2 | Comparative study of the inhibition of E. coli and murine aspartate transcarbamylase by phenobarbital analogues |
Escherichia coli |
| 2.1.3.2 | Comparative study of the inhibition of E. coli and murine aspartate transcarbamylase by phenobarbital analogues |
Mus musculus |
| 2.1.3.2 | Conformational plasticity of the active site entrance in E. coli aspartate transcarbamoylase and its implication in feedback regulation |
Escherichia coli |
| 2.1.3.2 | Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum |
Plasmodium falciparum |
| 2.1.3.2 | Identification of a non-competitive inhibitor of Plasmodium falciparum aspartate transcarbamoylase |
Plasmodium falciparum |
| 2.1.3.2 | New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development |
Homo sapiens |
| 2.1.3.2 | New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development |
Escherichia coli |
