Literature summary extracted from
Lampitella, E.; Landi, N.; Oliva, R.; Ragucci, S.; Petraccone, L.; Berisio, R.; Di Maro, A.; Del Vecchio, P.
Conformational stability of ageritin, a metal binding ribotoxin-like protein of fungal origin (2022), Int. J. Biol. Macromol., 221, 1012-1021.
General Stability
| EC Number |
General Stability |
Organism |
|---|
| 4.6.1.23 |
ageritin thermodynamic stability is related to Zn2+ ion binding at Cys18 |
Cyclocybe aegerita |
Inhibitors
| EC Number |
Inhibitors |
Comment |
Organism |
Structure |
|---|
| 4.6.1.23 |
additional information |
modification of the enzyme by alkylating the single Cys18 residue, which is predicted to bind Zn2+. S-pyridylethylated ageritin preserves both structure and activity, but S-pyridylethylated ageritin has low stability compared to the native protein |
Cyclocybe aegerita |
|
KM Value [mM]
| EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
|---|
| 4.6.1.23 |
additional information |
- |
additional information |
kinetics and thermodynamics of wild-type and modified S-pyridylethylated ageritin |
Cyclocybe aegerita |
|
Metals/Ions
| EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
|---|
| 4.6.1.23 |
Zn2+ |
required, ageritin thermodynamic stability is related to Zn2+ ion binding at Cys18 |
Cyclocybe aegerita |
|
Natural Substrates/ Products (Substrates)
| EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
|---|
| 4.6.1.23 |
rRNA + H2O |
Cyclocybe aegerita |
- |
? |
- |
? |
|
Organism
| EC Number |
Organism |
UniProt |
Comment |
Textmining |
|---|
| 4.6.1.23 |
Cyclocybe aegerita |
C0HLG3 |
Agrocybe aegerita |
- |
Substrates and Products (Substrate)
| EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
|---|
| 4.6.1.23 |
rRNA + H2O |
- |
Cyclocybe aegerita |
? |
- |
? |
|
Synonyms
| EC Number |
Synonyms |
Comment |
Organism |
|---|
| 4.6.1.23 |
ageritin |
- |
Cyclocybe aegerita |
| 4.6.1.23 |
ribotoxin-like protein |
- |
Cyclocybe aegerita |
Temperature Optimum [°C]
| EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
|---|
| 4.6.1.23 |
25 |
- |
assay at |
Cyclocybe aegerita |
Temperature Stability [°C]
| EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
|---|
| 4.6.1.23 |
78 |
- |
high protein thermal stability at all pHs with a denaturation temperature of 78°C |
Cyclocybe aegerita |
pH Optimum
| EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
|---|
| 4.6.1.23 |
5 |
- |
assay at |
Cyclocybe aegerita |
pH Stability
| EC Number |
pH Stability |
pH Stability Maximum |
Comment |
Organism |
|---|
| 4.6.1.23 |
4 |
7.4 |
ageritin is highly stable within this pH range |
Cyclocybe aegerita |
General Information
| EC Number |
General Information |
Comment |
Organism |
|---|
| 4.6.1.23 |
physiological function |
ageritin is a specific ribonuclease with major rRNA as target |
Cyclocybe aegerita |