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Literature summary for 2.3.1.87 extracted from

  • Cazamea-Catalan, D.; Magnanou, E.; Helland, R.; Vanegas, G.; Besseau, L.; Boeuf, G.; Paulin, C.H.; Joergensen, E.H.; Falcon, J.
    Functional diversity of Teleost arylalkylamine N-acetyltransferase-2: is the timezyme evolution driven by habitat temperature? (2012), Mol. Ecol., 21, 5027-5041.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Oncorhynchus mykiss
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Esox lucius
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Danio rerio
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Thunnus thynnus
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Salvelinus alpinus
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Arctogadus glacialis
AANAT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the GST-tagged enzyme from pGEX4T1 expression vector Oxydoras sifontesi

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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
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

Inhibitors

Inhibitors Comment Organism Structure
additional information strong substrate inhibition at 45°C Danio rerio
additional information strong substrate inhibition at 45°C Esox lucius
additional information strong substrate inhibition at 45°C Oncorhynchus mykiss
additional information strong substrate inhibition at 45°C Oxydoras sifontesi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information AANAT2 kinetic constants as a function of temperature, overview Danio rerio
additional information
-
additional information AANAT2 kinetic constants as a function of temperature, overview Salvelinus alpinus
additional information
-
additional information AANAT2 kinetic constants as a function of temperature, overview Oxydoras sifontesi
additional information
-
additional information AANAT2 kinetics in relation to temperature, overview Oncorhynchus mykiss
additional information
-
additional information AANAT2 kinetics in relation to temperature, overview Esox lucius

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + a 2-arylethylamine Oncorhynchus mykiss
-
CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine Esox lucius
-
CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine Danio rerio
-
CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine Salvelinus alpinus
-
CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine Oxydoras sifontesi
-
CoA + an N-acetyl-2-arylethylamine
-
?

Organism

Organism UniProt Comment Textmining
Arctogadus glacialis
-
-
-
Danio rerio
-
-
-
Esox lucius
-
-
-
Oncorhynchus mykiss
-
-
-
Oxydoras sifontesi
-
-
-
Salvelinus alpinus
-
-
-
Thunnus thynnus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Oncorhynchus mykiss
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Esox lucius
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Danio rerio
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Thunnus thynnus
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Salvelinus alpinus
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Arctogadus glacialis
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Oxydoras sifontesi

Source Tissue

Source Tissue Comment Organism Textmining
pineal gland
-
Oncorhynchus mykiss
-
pineal gland
-
Esox lucius
-
pineal gland
-
Danio rerio
-
pineal gland
-
Thunnus thynnus
-
pineal gland
-
Salvelinus alpinus
-
pineal gland
-
Arctogadus glacialis
-
pineal gland
-
Oxydoras sifontesi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + a 2-arylethylamine
-
Oncorhynchus mykiss CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine
-
Esox lucius CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine
-
Danio rerio CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine
-
Salvelinus alpinus CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + a 2-arylethylamine
-
Oxydoras sifontesi CoA + an N-acetyl-2-arylethylamine
-
?
acetyl-CoA + dopamine
-
Oncorhynchus mykiss CoA + N-acetyldopamine
-
?
acetyl-CoA + dopamine
-
Esox lucius CoA + N-acetyldopamine
-
?
acetyl-CoA + dopamine
-
Danio rerio CoA + N-acetyldopamine
-
?
acetyl-CoA + dopamine
-
Salvelinus alpinus CoA + N-acetyldopamine
-
?
acetyl-CoA + dopamine
-
Oxydoras sifontesi CoA + N-acetyldopamine
-
?
acetyl-CoA + phenylethylamine
-
Oncorhynchus mykiss CoA + N-acetylphenylethylamine
-
?
acetyl-CoA + phenylethylamine
-
Esox lucius CoA + N-acetylphenylethylamine
-
?
acetyl-CoA + phenylethylamine
-
Danio rerio CoA + N-acetylphenylethylamine
-
?
acetyl-CoA + phenylethylamine
-
Salvelinus alpinus CoA + N-acetylphenylethylamine
-
?
acetyl-CoA + phenylethylamine
-
Oxydoras sifontesi CoA + N-acetylphenylethylamine
-
?
acetyl-CoA + serotonin
-
Oncorhynchus mykiss CoA + N-acetylserotonin
-
?
acetyl-CoA + serotonin
-
Esox lucius CoA + N-acetylserotonin
-
?
acetyl-CoA + serotonin
-
Danio rerio CoA + N-acetylserotonin
-
?
acetyl-CoA + serotonin
-
Salvelinus alpinus CoA + N-acetylserotonin
-
?
acetyl-CoA + serotonin
-
Oxydoras sifontesi CoA + N-acetylserotonin
-
?
acetyl-CoA + tryptamine
-
Oncorhynchus mykiss CoA + N-acetyltryptamine
-
?
acetyl-CoA + tryptamine
-
Esox lucius CoA + N-acetyltryptamine
-
?
acetyl-CoA + tryptamine
-
Danio rerio CoA + N-acetyltryptamine
-
?
acetyl-CoA + tryptamine
-
Salvelinus alpinus CoA + N-acetyltryptamine
-
?
acetyl-CoA + tryptamine
-
Oxydoras sifontesi CoA + N-acetyltryptamine
-
?

Subunits

Subunits Comment Organism
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Oncorhynchus mykiss
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Esox lucius
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Danio rerio
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Thunnus thynnus
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Salvelinus alpinus
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Arctogadus glacialis
More AANAT2 primary to tertiary structures in relation to temperature, three-dimensional modeling, overview Oxydoras sifontesi

Synonyms

Synonyms Comment Organism
AANAT2
-
Oncorhynchus mykiss
AANAT2
-
Esox lucius
AANAT2
-
Danio rerio
AANAT2
-
Thunnus thynnus
AANAT2
-
Salvelinus alpinus
AANAT2
-
Arctogadus glacialis
AANAT2
-
Oxydoras sifontesi
arylalkylamine N-acetyltransferase-2
-
Oncorhynchus mykiss
arylalkylamine N-acetyltransferase-2
-
Esox lucius
arylalkylamine N-acetyltransferase-2
-
Danio rerio
arylalkylamine N-acetyltransferase-2
-
Thunnus thynnus
arylalkylamine N-acetyltransferase-2
-
Salvelinus alpinus
arylalkylamine N-acetyltransferase-2
-
Arctogadus glacialis
arylalkylamine N-acetyltransferase-2
-
Oxydoras sifontesi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
assay at Oncorhynchus mykiss
20
-
assay at Esox lucius
20
-
assay at Danio rerio
20
-
assay at Salvelinus alpinus
20
-
assay at Oxydoras sifontesi

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
AANAT2 primary to tertiary structures and kinetic constants as a function of temperature, overview Oncorhynchus mykiss
additional information
-
AANAT2 primary to tertiary structures and kinetic constants as a function of temperature, overview Esox lucius
additional information
-
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview Danio rerio
additional information
-
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview Salvelinus alpinus
additional information
-
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview Oxydoras sifontesi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
5 min, loss of 60% activity Esox lucius
45
-
5 min, loss of 60% activity Danio rerio
45
-
10 min, loss of 25% activity, 50% after 40 min Oxydoras sifontesi
45
-
10 min, loss of 60% activity Salvelinus alpinus
45 65 5 min, complete inactivation Oncorhynchus mykiss
65
-
5 min, complete loss of activity Esox lucius
65
-
5 min, complete loss of activity Danio rerio
65
-
5 min, complete loss of activity Salvelinus alpinus
65
-
10 min, loss of 65% activity, 60% after 40 min Oxydoras sifontesi

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Oncorhynchus mykiss
acetyl-CoA
-
Esox lucius
acetyl-CoA
-
Danio rerio
acetyl-CoA
-
Thunnus thynnus
acetyl-CoA
-
Salvelinus alpinus
acetyl-CoA
-
Arctogadus glacialis
acetyl-CoA
-
Oxydoras sifontesi

General Information

General Information Comment Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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