Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | integral membrane enzyme | Rattus norvegicus | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylcholine + H2O | Rattus norvegicus | - |
choline + acetate | - |
? | |
acetylcholine + H2O | Rattus norvegicus Wistar | - |
choline + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P37136 | - |
- |
Rattus norvegicus Wistar | P37136 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
erythrocyte | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylcholine + H2O | - |
Rattus norvegicus | choline + acetate | - |
? | |
acetylcholine + H2O | - |
Rattus norvegicus Wistar | choline + acetate | - |
? | |
acetylthiocholine + H2O | activity of AChE is determined by Ellman's method using acetylthiocholine iodide as a substrate | Rattus norvegicus | thiocholine + acetate | - |
? | |
acetylthiocholine + H2O | activity of AChE is determined by Ellman's method using acetylthiocholine iodide as a substrate | Rattus norvegicus Wistar | thiocholine + acetate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AChE | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
kinetics of thermal denaturation of acetylcholinesterase of the rat red blood cell membrane during moderate hypothermia, thermostability of acetylcholinesterase of rat erythrocyte membranes in the norm and moderate hypothermia, detailed overview. Kinetics of the thermal denaturation of acetylcholinesterase are nonlinear and correspond to a model that involves two-step denaturation, fast and slow, of the enzyme's native form. The rate constants of the fast phase, k1, are much higher than those of the slow phase, k2, while the energy of the fast phase activation is lower by only 19.4% compared to that of the slow one. Short-term moderate hypothermia increases k1 and decreases the index of relative activity of the intermediate form of acetylcholinesterase (parameter beta), leading to significant lowering of the activation energies of both stages, parameter beta becomes more temperature-dependent. The prolongation of hypothermia up to 3 h mainly contributes to a decrease in k1 and k2 relative to short-term hypothermia and the activation energy of denaturation increases. The structure of acetylcholinesterase is labilized at the initial stages of the development of the hypothermic state and stabilized during prolonged hypothermia. Molecular mechanisms of the changes in the thermal stability of erythrocyte AChE | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
additional information | molecular mechanisms of the changes in the thermal stability of erythrocyte AChE, overview. H2O2 can play a regulatory role in the functioning of AChE | Rattus norvegicus |