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Literature summary 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)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

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
-
-
-

Reaction

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
a
2.3.1.87 acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Esox lucius
a
2.3.1.87 acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Danio rerio
a
2.3.1.87 acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Thunnus thynnus
a
2.3.1.87 acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Salvelinus alpinus
a
2.3.1.87 acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Arctogadus glacialis
a
2.3.1.87 acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine catalytic reaction mechanism, overview Oxydoras sifontesi
a

Source Tissue

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
-

Substrates and Products (Substrate)

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
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

Cofactor

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

General Information

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