Any feedback?
Literature summary for 3.4.11.1 extracted from
- Characterization of activity of a potential food-grade leucine aminopeptidase from kiwifruit (2010), Enzyme Res., 2010, 517283.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Actinidia deliciosa | - |
cv. Hayward | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate precipitation, ion exchange chromatography (DEAE cellulose): suggesting at least the presence of two isoenzymes (adsorbed and unadsorbed fractions) | Actinidia deliciosa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fruit | - |
Actinidia deliciosa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-leucine-4-nitroanilide + H2O | - |
Actinidia deliciosa | L-leucine + 4-nitroaniline | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| leucine aminopeptidase | - |
Actinidia deliciosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
two values suggest two isoenzymes | Actinidia deliciosa |
| 50 | - |
two values suggest two isoenzymes | Actinidia deliciosa |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
after 30 min activity reduced to 63% (100% at 37°C) | Actinidia deliciosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Actinidia deliciosa |
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
