EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.1.7 | 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide | BW284c51, a specific inhibitor of AChE | Gambusia yucatana | |
3.1.1.7 | eserine | - |
Gambusia yucatana | |
3.1.1.8 | 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide | BW284c51 | Gambusia yucatana | |
3.1.1.8 | eserine | - |
Gambusia yucatana |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.1.7 | additional information | - |
additional information | Michaelis-Menten kinetics | Gambusia yucatana | |
3.1.1.7 | 2.38 | - |
acetylthiocholine | enzyme from head, pH 7.4, temperature not specified in the publication | Gambusia yucatana | |
3.1.1.7 | 5.47 | - |
acetylthiocholine | enzyme from muscle, pH 7.4, temperature not specified in the publication | Gambusia yucatana | |
3.1.1.8 | additional information | - |
additional information | Michaelis-Menten kinetics | Gambusia yucatana | |
3.1.1.8 | 0.55 | - |
butyrylthiocholine | enzyme from muscle, pH 7.4, temperature not specified in the publication | Gambusia yucatana | |
3.1.1.8 | 1.24 | - |
butyrylthiocholine | enzyme from head, pH 7.4, temperature not specified in the publication | Gambusia yucatana |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.7 | acetylcholine + H2O | Gambusia yucatana | - |
choline + acetate | - |
? | |
3.1.1.8 | butyrylcholine + H2O | Gambusia yucatana | - |
choline + butyrate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.7 | Gambusia yucatana | - |
from Yucatan Peninsula, Mexico | - |
3.1.1.8 | Gambusia yucatana | - |
from Yucatan Peninsula, Mexico | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.1.7 | head | - |
Gambusia yucatana | - |
3.1.1.7 | muscle | - |
Gambusia yucatana | - |
3.1.1.8 | head | - |
Gambusia yucatana | - |
3.1.1.8 | additional information | the ChE presented in head and muscle is able to hydrolyze ASChI and BSChI obtaining higher Vmax and Km with ASChI. This suggests that the ChE present in head and muscle have high affinity for BSChI (ASChI Km < BSChI Km) but is poorly hydrolyzed. With ASChI as substrate, a relatively high enzyme activity is obtained (ASChI Vmax > BSChI Vmax), but it has a smaller affinity for the enzyme with respect to BSChI | Gambusia yucatana | - |
3.1.1.8 | muscle | - |
Gambusia yucatana | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.1.7 | 0.12024 | - |
pH 7.4, temperature not specified in the publication | Gambusia yucatana |
3.1.1.8 | 0.00595 | - |
crude enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.7 | acetylcholine + H2O | - |
Gambusia yucatana | choline + acetate | - |
? | |
3.1.1.7 | acetylthiocholine + H2O | - |
Gambusia yucatana | thiocholine + acetate | - |
? | |
3.1.1.8 | butyrylcholine + H2O | - |
Gambusia yucatana | choline + butyrate | - |
? | |
3.1.1.8 | butyrylthiocholine + H2O | - |
Gambusia yucatana | thiocholine + butyrate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.7 | AChE | - |
Gambusia yucatana |
3.1.1.8 | BChE | - |
Gambusia yucatana |
3.1.1.8 | butyrylcholinesterase | - |
Gambusia yucatana |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.7 | 7.4 | - |
assay at | Gambusia yucatana |
3.1.1.8 | 7.4 | - |
assay at | Gambusia yucatana |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
3.1.1.7 | 0.00005 | - |
head enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide | |
3.1.1.7 | 0.00006 | - |
muscle enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide | |
3.1.1.7 | 0.00022 | - |
head enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | eserine | |
3.1.1.7 | 0.00033 | - |
muscle enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | eserine | |
3.1.1.8 | 0.00007 | - |
head enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | eserine | |
3.1.1.8 | 0.00009 | - |
muscle enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | eserine | |
3.1.1.8 | 0.00014 | - |
muscle enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide | |
3.1.1.8 | 0.00037 | - |
head enzyme, pH 7.4, temperature not specified in the publication | Gambusia yucatana | 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.1.7 | physiological function | acetylcholinesterase (AChE) is a very important enzyme in the nervous system because it hydrolyzes acetylcholine in synaptic functions. Relationship between cholinesterase activity and total length or sex in wild Gambusia yucatana from different water bodies in the Yucatan Peninsula, Mexiko | Gambusia yucatana |