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Literature summary for 3.1.1.7 extracted from

  • Klichkhanov, N.; Dzhafarova, A.
    The kinetics of thermal denaturation of acetylcholinesterase of the rat red blood cell membrane during moderate hypothermia (2018), Biophysics, 63, 526-536 .
No PubMed abstract available
Search for more literature for 3.1.1.7

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane enzyme Rattus norvegicus 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylcholine + H2O Rattus norvegicus
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 choline + acetate
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 ?
acetylcholine + H2O Rattus norvegicus Wistar
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 choline + acetate
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P37136
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Rattus norvegicus Wistar P37136
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Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
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 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylcholine + H2O
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 Rattus norvegicus choline + acetate
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 ?
acetylcholine + H2O
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 Rattus norvegicus Wistar choline + acetate
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 ?
acetylthiocholine + H2O activity of AChE is determined by Ellman's method using acetylthiocholine iodide as a substrate Rattus norvegicus thiocholine + acetate
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acetylthiocholine + H2O activity of AChE is determined by Ellman's method using acetylthiocholine iodide as a substrate Rattus norvegicus Wistar thiocholine + acetate
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 ?

Synonyms

Synonyms Comment Organism
AChE
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 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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 assay at Rattus norvegicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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 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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
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 assay at Rattus norvegicus

General Information

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