Any feedback?
Literature summary extracted from
- Mechanisms of the aspartoacylase catalytic activity regulation according to the computer modeling results (2018), Moscow Univ. Chem. Bull., 73, 152-154 .
No PubMed abstract available
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.5.1.15 | K213E | the point mutation does not affect the catalytic function of the enzyme | Homo sapiens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.15 | Homo sapiens | P45381 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.15 | N-acetyl-L-aspartate + H2O | - |
Homo sapiens | acetate + L-aspartate | - |
? |  |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
