EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
|---|
   3.5.1.15 | 754252 |
Allosteric control of N-acetyl-aspartate hydrolysis by the Y231C and F295S mutants of human aspartoacylase |
J. Chem. Inf. Model. |
59 |
2299-2308 |
2019 |
Homo sapiens |
30431265 |
| 3.5.1.15 | 755390 |
Aspartoacylase A central nervous system enzyme. Structure, catalytic activity and regulation mechanisms |
Russ. Chem. Rev. |
88 |
1-26 |
2019 |
Homo sapiens |
- |
| 3.5.1.15 | 754618 |
Comparative computational assessment of the pathogenicity of mutations in the aspartoacylase enzyme |
Metab. Brain Dis. |
32 |
2105-2118 |
2017 |
Homo sapiens |
28879565 |
| 3.5.1.15 | 754806 |
Mechanisms of the aspartoacylase catalytic activity regulation according to the computer modeling results |
Moscow Univ. Chem. Bull. |
73 |
152-154 |
2018 |
Homo sapiens |
- |
| 3.5.1.15 | 754250 |
Role of protein dimeric interface in allosteric inhibition of N-acetyl-aspartate hydrolysis by human aspartoacylase |
J. Chem. Inf. Model. |
57 |
1999-2008 |
2017 |
Homo sapiens |
28737906 |
| 3.5.1.15 | 754480 |
Three faces of N-acetylaspartate activator, substrate, and inhibitor of human aspartoacylase |
J. Phys. Chem. B |
121 |
9389-9397 |
2017 |
Homo sapiens |
28903559 |
| 3.5.1.15 | 719318 |
A general acid-general base reaction mechanism for human brain aspartoacylase: A QM/MM study |
Comput. Theoret. Chem. |
980 |
85-91 |
2012 |
Homo sapiens |
- |
| 3.5.1.15 | 679264 |
A new T677C mutation of the aspartoacylase gene encodes for a protein with no enzymatic activity |
Clin. Biochem. |
41 |
611-615 |
2008 |
Homo sapiens |
18280251 |
| 3.5.1.15 | 719532 |
A novel aspartoacylase (ASPA) gene mutation in Canavan disease |
Fetal. Pediatr. Pathol. |
31 |
236-239 |
2012 |
Homo sapiens |
22468686 |
| 3.5.1.15 | 208998 |
A radiochemical assay for N-acetyl-L-aspartate amidohydrolase (EC 3.5.1.15) and its occurrence in the tissues of the chicken |
Life Sci. |
23 |
791-796 |
1978 |
Columba sp. |
703517 |
