Any feedback?
Literature summary extracted from
- N-terminal domain of Pyrococcus furiosus L-asparaginase functions as a non-specific, stable, molecular chaperone (2013), FEBS J., 280, 2688-2699.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.1 | expression in Escherichia coli | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.1 | Pyrococcus furiosus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.1 | - |
Pyrococcus furiosus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.1 | additional information | the N-terminal domain of L-asparaginase functions as a non-specific, stable, molecular chaperone | Pyrococcus furiosus | ? | - |
? |  |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.1 | dimer | the enzyme functions as a dimer with each monomer consisting of distinct N- and C-terminal domains (NPfA and CPfA, respectively), connected by a linker | Pyrococcus furiosus |
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
