EC Number   |
Title |
Organism |
|---|
   3.5.1.15 | Allosteric control of N-acetyl-aspartate hydrolysis by the Y231C and F295S mutants of human aspartoacylase |
Homo sapiens |
| 3.5.1.15 | Aspartoacylase A central nervous system enzyme. Structure, catalytic activity and regulation mechanisms |
Homo sapiens |
| 3.5.1.15 | Comparative computational assessment of the pathogenicity of mutations in the aspartoacylase enzyme |
Homo sapiens |
| 3.5.1.15 | Mechanisms of the aspartoacylase catalytic activity regulation according to the computer modeling results |
Homo sapiens |
| 3.5.1.15 | Role of protein dimeric interface in allosteric inhibition of N-acetyl-aspartate hydrolysis by human aspartoacylase |
Homo sapiens |
| 3.5.1.15 | Three faces of N-acetylaspartate activator, substrate, and inhibitor of human aspartoacylase |
Homo sapiens |
| 3.5.1.15 | A general acid-general base reaction mechanism for human brain aspartoacylase: A QM/MM study |
Homo sapiens |
| 3.5.1.15 | A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity |
Homo sapiens |
| 3.5.1.15 | A novel aspartoacylase (ASPA) gene mutation in Canavan disease |
Homo sapiens |
| 3.5.1.15 | A radiochemical assay for N-acetyl-L-aspartate amidohydrolase (EC 3.5.1.15) and its occurrence in the tissues of the chicken |
Columba sp. |
