EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Oncorhynchus mykiss |
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Esox lucius |
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Danio rerio |
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Thunnus thynnus |
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Salvelinus alpinus |
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Arctogadus glacialis |
2.3.1.87 | AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector | Oxydoras sifontesi |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Oncorhynchus mykiss |
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Esox lucius |
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Danio rerio |
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Thunnus thynnus |
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Salvelinus alpinus |
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Arctogadus glacialis |
2.3.1.87 | additional information | AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns | Oxydoras sifontesi |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.87 | additional information | strong substrate inhibition at 45°C | Danio rerio | |
2.3.1.87 | additional information | strong substrate inhibition at 45°C | Esox lucius | |
2.3.1.87 | additional information | strong substrate inhibition at 45°C | Oncorhynchus mykiss | |
2.3.1.87 | additional information | strong substrate inhibition at 45°C | Oxydoras sifontesi |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.87 | additional information | - |
additional information | AANAT2 kinetic constants as a function of temperature, overview | Danio rerio | |
2.3.1.87 | additional information | - |
additional information | AANAT2 kinetic constants as a function of temperature, overview | Salvelinus alpinus | |
2.3.1.87 | additional information | - |
additional information | AANAT2 kinetic constants as a function of temperature, overview | Oxydoras sifontesi | |
2.3.1.87 | additional information | - |
additional information | AANAT2 kinetics in relation to temperature, overview | Oncorhynchus mykiss | |
2.3.1.87 | additional information | - |
additional information | AANAT2 kinetics in relation to temperature, overview | Esox lucius |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | Oncorhynchus mykiss | - |
CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | Esox lucius | - |
CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | Danio rerio | - |
CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | Salvelinus alpinus | - |
CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | Oxydoras sifontesi | - |
CoA + an N-acetyl-2-arylethylamine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.87 | Arctogadus glacialis | - |
- |
- |
2.3.1.87 | Danio rerio | - |
- |
- |
2.3.1.87 | Esox lucius | - |
- |
- |
2.3.1.87 | Oncorhynchus mykiss | - |
- |
- |
2.3.1.87 | Oxydoras sifontesi | - |
- |
- |
2.3.1.87 | Salvelinus alpinus | - |
- |
- |
2.3.1.87 | Thunnus thynnus | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Oncorhynchus mykiss | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Esox lucius | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Danio rerio | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Thunnus thynnus | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Salvelinus alpinus | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Arctogadus glacialis | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine | catalytic reaction mechanism, overview | Oxydoras sifontesi |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.3.1.87 | pineal gland | - |
Oncorhynchus mykiss | - |
2.3.1.87 | pineal gland | - |
Esox lucius | - |
2.3.1.87 | pineal gland | - |
Danio rerio | - |
2.3.1.87 | pineal gland | - |
Thunnus thynnus | - |
2.3.1.87 | pineal gland | - |
Salvelinus alpinus | - |
2.3.1.87 | pineal gland | - |
Arctogadus glacialis | - |
2.3.1.87 | pineal gland | - |
Oxydoras sifontesi | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | - |
Oncorhynchus mykiss | CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | - |
Esox lucius | CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | - |
Danio rerio | CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | - |
Salvelinus alpinus | CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + a 2-arylethylamine | - |
Oxydoras sifontesi | CoA + an N-acetyl-2-arylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + dopamine | - |
Oncorhynchus mykiss | CoA + N-acetyldopamine | - |
? | |
2.3.1.87 | acetyl-CoA + dopamine | - |
Esox lucius | CoA + N-acetyldopamine | - |
? | |
2.3.1.87 | acetyl-CoA + dopamine | - |
Danio rerio | CoA + N-acetyldopamine | - |
? | |
2.3.1.87 | acetyl-CoA + dopamine | - |
Salvelinus alpinus | CoA + N-acetyldopamine | - |
? | |
2.3.1.87 | acetyl-CoA + dopamine | - |
Oxydoras sifontesi | CoA + N-acetyldopamine | - |
? | |
2.3.1.87 | acetyl-CoA + phenylethylamine | - |
Oncorhynchus mykiss | CoA + N-acetylphenylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + phenylethylamine | - |
Esox lucius | CoA + N-acetylphenylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + phenylethylamine | - |
Danio rerio | CoA + N-acetylphenylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + phenylethylamine | - |
Salvelinus alpinus | CoA + N-acetylphenylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + phenylethylamine | - |
Oxydoras sifontesi | CoA + N-acetylphenylethylamine | - |
? | |
2.3.1.87 | acetyl-CoA + serotonin | - |
Oncorhynchus mykiss | CoA + N-acetylserotonin | - |
? | |
2.3.1.87 | acetyl-CoA + serotonin | - |
Esox lucius | CoA + N-acetylserotonin | - |
? | |
2.3.1.87 | acetyl-CoA + serotonin | - |
Danio rerio | CoA + N-acetylserotonin | - |
? | |
2.3.1.87 | acetyl-CoA + serotonin | - |
Salvelinus alpinus | CoA + N-acetylserotonin | - |
? | |
2.3.1.87 | acetyl-CoA + serotonin | - |
Oxydoras sifontesi | CoA + N-acetylserotonin | - |
? | |
2.3.1.87 | acetyl-CoA + tryptamine | - |
Oncorhynchus mykiss | CoA + N-acetyltryptamine | - |
? | |
2.3.1.87 | acetyl-CoA + tryptamine | - |
Esox lucius | CoA + N-acetyltryptamine | - |
? | |
2.3.1.87 | acetyl-CoA + tryptamine | - |
Danio rerio | CoA + N-acetyltryptamine | - |
? | |
2.3.1.87 | acetyl-CoA + tryptamine | - |
Salvelinus alpinus | CoA + N-acetyltryptamine | - |
? | |
2.3.1.87 | acetyl-CoA + tryptamine | - |
Oxydoras sifontesi | CoA + N-acetyltryptamine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Oncorhynchus mykiss |
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Esox lucius |
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Danio rerio |
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Thunnus thynnus |
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Salvelinus alpinus |
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Arctogadus glacialis |
2.3.1.87 | More | AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview | Oxydoras sifontesi |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.87 | AANAT2 | - |
Oncorhynchus mykiss |
2.3.1.87 | AANAT2 | - |
Esox lucius |
2.3.1.87 | AANAT2 | - |
Danio rerio |
2.3.1.87 | AANAT2 | - |
Thunnus thynnus |
2.3.1.87 | AANAT2 | - |
Salvelinus alpinus |
2.3.1.87 | AANAT2 | - |
Arctogadus glacialis |
2.3.1.87 | AANAT2 | - |
Oxydoras sifontesi |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Oncorhynchus mykiss |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Esox lucius |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Danio rerio |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Thunnus thynnus |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Salvelinus alpinus |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Arctogadus glacialis |
2.3.1.87 | arylalkylamine N-acetyltransferase-2 | - |
Oxydoras sifontesi |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.87 | 20 | - |
assay at | Oncorhynchus mykiss |
2.3.1.87 | 20 | - |
assay at | Esox lucius |
2.3.1.87 | 20 | - |
assay at | Danio rerio |
2.3.1.87 | 20 | - |
assay at | Salvelinus alpinus |
2.3.1.87 | 20 | - |
assay at | Oxydoras sifontesi |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.87 | additional information | - |
AANAT2 primary to tertiary structures and kinetic constants as a function of temperature, overview | Oncorhynchus mykiss |
2.3.1.87 | additional information | - |
AANAT2 primary to tertiary structures and kinetic constants as a function of temperature, overview | Esox lucius |
2.3.1.87 | additional information | - |
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview | Danio rerio |
2.3.1.87 | additional information | - |
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview | Salvelinus alpinus |
2.3.1.87 | additional information | - |
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview | Oxydoras sifontesi |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.87 | 45 | - |
5 min, loss of 60% activity | Esox lucius |
2.3.1.87 | 45 | - |
5 min, loss of 60% activity | Danio rerio |
2.3.1.87 | 45 | - |
10 min, loss of 25% activity, 50% after 40 min | Oxydoras sifontesi |
2.3.1.87 | 45 | - |
10 min, loss of 60% activity | Salvelinus alpinus |
2.3.1.87 | 45 | 65 | 5 min, complete inactivation | Oncorhynchus mykiss |
2.3.1.87 | 65 | - |
5 min, complete loss of activity | Esox lucius |
2.3.1.87 | 65 | - |
5 min, complete loss of activity | Danio rerio |
2.3.1.87 | 65 | - |
5 min, complete loss of activity | Salvelinus alpinus |
2.3.1.87 | 65 | - |
10 min, loss of 65% activity, 60% after 40 min | Oxydoras sifontesi |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.87 | acetyl-CoA | - |
Oncorhynchus mykiss | |
2.3.1.87 | acetyl-CoA | - |
Esox lucius | |
2.3.1.87 | acetyl-CoA | - |
Danio rerio | |
2.3.1.87 | acetyl-CoA | - |
Thunnus thynnus | |
2.3.1.87 | acetyl-CoA | - |
Salvelinus alpinus | |
2.3.1.87 | acetyl-CoA | - |
Arctogadus glacialis | |
2.3.1.87 | acetyl-CoA | - |
Oxydoras sifontesi |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Oncorhynchus mykiss |
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Esox lucius |
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Danio rerio |
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Thunnus thynnus |
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Salvelinus alpinus |
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Arctogadus glacialis |
2.3.1.87 | evolution | AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature | Oxydoras sifontesi |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Oncorhynchus mykiss |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Esox lucius |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Danio rerio |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Thunnus thynnus |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Salvelinus alpinus |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Arctogadus glacialis |
2.3.1.87 | physiological function | arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature | Oxydoras sifontesi |