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Enzyme Nomenclature
Information on EC 2.3.1.87 - aralkylamine N-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.87
Word Map on EC 2.3.1.87
- 2.3.1.87
- melatonin
-
pineal
- gland
- rhythm
-
circadian
- retina
-
clock
-
night
-
nocturnal
- pinealocytes
- norepinephrine
- hydroxyindole-o-methyltransferase
- hiomt
-
oscillator
- photoreceptors
-
photoperiodic
-
suprachiasmatic
-
diurnal
-
arylalkylamine-n-acetyltransferase
-
adrenergic
-
light-dark
- scn
- tryptamine
-
entrain
-
photic
-
zeitgeber
-
night-time
-
day-night
- n-acetyl-5-methoxytryptamine
- octopamine
- analysis
- phenylethylamines
-
arylamine
-
ne-stimulated
-
gcn5-related
-
hydroxyindole
-
rhythm-generating
-
gnat
-
acetylserotonin
-
photoreceptive
- medicine
-
extrapineal
-
clock-controlled
-
melatonin-synthesizing
-
clockwork
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.87
-
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RECOMMENDED NAME
GeneOntology No.
aralkylamine N-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
mechanism
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
ordered bi-bi sequential mechanism
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
catalytic reaction mechanism, overview
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
mechanism
-
-
acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:2-arylethylamine N-acetyltransferase
Narrow specificity towards 2-arylethylamines, including serotonin (5-hydroxytryptamine), tryptamine, 5-methoxytryptamine and phenylethylamine. This is the penultimate enzyme in the production of melatonin (5-methoxy-N-acetyltryptamine) and controls its synthesis (cf. EC 2.1.1.4, acetylserotonin O-methyltransferase). Differs from EC 2.3.1.5 arylamine N-acetyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
92941-56-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from NGM plates seeded with Escherichia coli NA22
UniProt
collected from NGM plates seeded with Escherichia coli NA22
UniProt
collected from an apple, Malus pumila, cv. Fuji, orchard at Akita, Japan
-
-
arylalkylamine N-acetyltransferase long mutant, i.e. arylalkylamine N-acetyltransferase type 2 protein
UniProt
arylalkylamine N-acetyltransferase short mutant, i.e. arylalkylamine N-acetyltransferase type 1 protein
UniProt
arylalkylamine N-acetyltransferase wild-type; strains Dazao and C108
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
the abnormal Bm-iAANAT is responsible for the mln mutant, phenotype, overview. The content of dopamine in the mln mutant is about 2times higher than in the wild-type. A greater accumulation of dopamine results from the functional deficiency of Bm-iAANAT in the mutant and that the excessive dopamine is converted into dopamine melanin, causing the darker color pattern of the sclerified regions in the mln mutant compared with the wild-type; the abnormal Bm-iAANAT is responsible for the mln mutant, phenotype, overview. The content of dopamine in the mln mutant is about 2times higher than in the wild-type. A greater accumulation of dopamine results from the functional deficiency of Bm-iAANAT in the mutant and that the excessive dopamine is converted into dopamine melanin, causing the darker color pattern of the sclerified regions in the mln mutant compared with the wild-type
metabolism
physiological function
additional information
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
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
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
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
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
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
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
evolution
evolution of insect arylalkylamine N-acetyltransferases, structural evidence from the yellow fever mosquito, Aedes aegypti, overview
metabolism
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis, melatonin biosynthesis pathway overview
metabolism
-
the enzyme catalyzes the first step in melatonin biosynthesis, melatonin biosynthesis follows a 24 h day and night rhythm, which is different in fasted, fed, and refed fish, overview
metabolism
-
the enzyme catalyzes the first step in melatonin biosynthesis, melatonin biosynthesis follows a 24 h day and night rhythm, which is different in fasted, fed, and refed fish, overview
metabolism
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis
metabolism
-
arylalkylamine N-acetyltransferase is the rate-limiting enzyme of the melatonin biosynthesis pathway
metabolism
-
serotonin N-acetyltransferase is a rate-limiting enzyme in melatonin biosynthesis in vertebrates
physiological function
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis, melatonin is a hormone acting as a synchronizer for the circadian system, overview. Evolution of the pineal gland and the circadian system involving melatonin, overview
physiological function
-
AANAT is a key circadian rhythm enzyme that drives the nocturnal production of melatonin in the pineal
physiological function
-
Aanat2 is the main enzyme responsible of the plasma nocturnal melatonin increase in the fish
physiological function
-
the melatonin synthetic enzyme arylalkylamine N-acetyltransferase is a significant element in a possible reactive oxygen species removal system. UV signals initiate melatonin synthesis for reactive oxgene species removal in mites
physiological function
arylalkylamine-N-acetyltransferases play a role in color pattern mutation in Lepidoptera, the BmiAANAT gene plays an essential role in the pigment metabolism in silkworm; arylalkylamine-N-acetyltransferases play a role in color pattern mutation in Lepidoptera, the BmiAANAT gene plays an essential role in the pigment metabolism in silkworm; arylalkylamine-N-acetyltransferases play a role in color pattern mutation in Lepidoptera, the BmiAANAT gene plays an essential role in the pigment metabolism in silkworm
physiological function
-
serotonin N-acetyltransferase is responsible for the production of N-acetylserotonin, an intermediate of melatonin biosynthesis. Melatonin, i.e. N-acetyl-5-methoxytryptamine, has multiple functions in vertebrates, including the regulation of circadian rhythms and photoperiodism. Plant melatonin is involved in cold stress
physiological function
melatonin influences circadian rhythms and seasonal behavioral changes in vertebrates, it is synthesized from serotonin by N-acetylation by arylalkylamine N-acetyltransferase and O-methylation by N-acetylserotonin methyltransferase, EC 2.1.1.4
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
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
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
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
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
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
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
physiological function
aaNATs are involved in sclerotization and neurotransmitter inactivation in insects
physiological function
suppression of gene expression leads to melanin deposition in the head and integument. An increase in dopamine levels affects melanism patterns on the heads of transgenic worms. A reduction in the enzyme activity of AANAT leads to changes in dopamine levels
physiological function
isoform AANATL2 has a role in the biosynthetic formation of long-chain N-acylserotonins and N-acydopamines
physiological function
A0A0K1H4R1;, B9TU30;, B9TU31;
Aanat1 isoforms have a broad range of functions including melatonin synthesis in the retina, and catabolism of serotonin and dopamine in the retina and other tissues; Aanat1 isoforms have a broad range of functions including melatonin synthesis in the retina, and catabolism of serotonin and dopamine in the retina and other tissues; isoform Aanat2 is a pineal enzyme involved in melatonin production
physiological function
isoform AANAT1 is an important enzyme in the regulation of dopamine and N-acetyldopamine content in liver
physiological function
-
melatonin influences circadian rhythms and seasonal behavioral changes in vertebrates, it is synthesized from serotonin by N-acetylation by arylalkylamine N-acetyltransferase and O-methylation by N-acetylserotonin methyltransferase, EC 2.1.1.4
-
additional information
-
under light-dark conditions, a rhythmic pattern of melatonin levels occurs with higher levels toward the middle of the night, peaking at zeitgeber time ZT18, and with a minimum value around ZT0-6. AA-NAT activity shows a diurnal and circadian fluctuation with higher levels of activity during the early night, both under light-dark conditions and constant darkness conditions. A peak is found around ZT12 and circadian time CT12. Light acts on AA-NAT through a well-known phototransduction mechanism that originates in the retina, is mediated by the retinohypothalamic tract, and processed in the hypothalamic suprachiasmatic nuclei, SCN, the site of the master circadian clock. From the SCN, the photic message is transduced through the sympathetic nervous system to the pineal, where noradrenergic receptors, among others, control the activity of AA-NAT
additional information
under light-dark conditions, a rhythmic pattern of melatonin levels occurs with higher levels toward the middle of the night, peaking at zeitgeber time ZT18, and with a minimum value around ZT0-6. AA-NAT activity shows a diurnal and circadian fluctuation with higher levels of activity during the early night, both under light-dark conditions and constant darkness conditions. A peak is found around ZT12 and circadian time CT12. Light acts on AA-NAT through a well-known phototransduction mechanism that originates in the retina, is mediated by the retinohypothalamic tract, and processed in the hypothalamic suprachiasmatic nuclei, SCN, the site of the master circadian clock. From the SCN, the photic message is transduced through the sympathetic nervous system to the pineal, where noradrenergic receptors, among others, control the activity of AA-NAT
additional information
-
three clusters of aaNAT-like sequences in insects: typical insect aaNAT, polyamine NAT-like aaNAT, and mosquito unique putative aaNAT, paaNAT. aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
additional information
three clusters of aaNAT-like sequences in insects: typical insect aaNAT, polyamine NAT-like aaNAT, and mosquito unique putative aaNAT, paaNAT. aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
additional information
-
under light-dark conditions, a rhythmic pattern of melatonin levels occurs with higher levels toward the middle of the night, peaking at zeitgeber time ZT18, and with a minimum value around ZT0-6. AA-NAT activity shows a diurnal and circadian fluctuation with higher levels of activity during the early night, both under light-dark conditions and constant darkness conditions. A peak is found around ZT12 and circadian time CT12. Light acts on AA-NAT through a well-known phototransduction mechanism that originates in the retina, is mediated by the retinohypothalamic tract, and processed in the hypothalamic suprachiasmatic nuclei, SCN, the site of the master circadian clock. From the SCN, the photic message is transduced through the sympathetic nervous system to the pineal, where noradrenergic receptors, among others, control the activity of AA-NAT
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 2,5-dimethoxyphenylethylamine
CoA + ?
24% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2,5-dimethoxyphenylethylamine
CoA + N-acetyl-2,5-dimethoxyphenylethylamine
-
68% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(2,3-dichlorophenyl)-ethylamine
CoA + N-acetyl-2-(2,3-dichlorophenyl)-ethylamine
acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine
acetyl-CoA + 2-(3,4-dimethoxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dimethoxyphenyl)-ethylamine
acetyl-CoA + 2-fluorophenylethylamine
CoA + ?
69% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-fluorophenylethylamine
CoA + N-acetyl-2-fluorophenylethylamine
-
52% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-(trifluoromethyl)phenethylamine
CoA + N-acetyl-3-(trifluoromethyl)phenethylamine
-
-
-
-
?
acetyl-CoA + 3-hydroxy-4-methoxyphenethylamine
CoA + ?
1% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-hydroxy-4-methoxyphenethylamine
CoA + N-acetyl-3-hydroxy-4-methoxyphenethylamine
-
7.2% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-hydroxyphenethylamine
CoA + ?
24% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-hydroxyphenethylamine
CoA + N-acetyl-3-hydroxyphenethylamine
-
36% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-indolebutylamine
CoA + N-acetyl-(3-indol-3-yl-butyl)-amine
-
60-fold less efficiently than serotonin
-
-
?
acetyl-CoA + 3-indolepropylamine
CoA + N-acetyl-(3-indol-3-yl-propyl)-amine
-
20-fold less efficiently than serotonin
-
-
?
acetyl-CoA + 3-methoxy-2-phenylethylamine
CoA + ?
23% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-methoxy-2-phenylethylamine
CoA + N-acetyl-3-methoxy-2-phenylethylamine
-
55% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-methoxyphenethylamine
CoA + N-acetyl-3-methoxyphenethylamine
-
-
-
-
?
acetyl-CoA + 3-methoxytyramine
CoA + ?
17% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 3-methoxytyramine
CoA + N-acetyl-3-methoxytyramine
-
73% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonamide
CoA + ?
-
1% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 5-benzyloxytryptamine
CoA + N-acetyl-5-benzyloxytryptamine
-
-
-
-
?
acetyl-CoA + 5-hydroxydopamine
CoA + N-acetyl-5-hydroxydopamine
-
4.4% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 6-hydroxydopamine
CoA + ?
51% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 6-hydroxydopamine
CoA + N-acetyl-6-hydroxydopamine
-
1.5% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + alpha-methyltryptamine
CoA + N-acetyl-alpha-methyltryptamine
-
racemic, 9:1 stereoselectivity for R-enantiomer, less efficiently than serotonin
-
-
?
acetyl-CoA + beta-methylphenethylamine
CoA + N-acetyl-beta-methylphenethylamine
-
-
-
-
?
acetyl-CoA + Nomega-methyltryptamine
CoA + ?
-
less efficiently than serotonin
-
-
?
acetyl-CoA + phenylethylamine
N-acetyl-phenylethylamine
-
-
-
?
acetyl-CoA + tryptophol
CoA + N-acetyltryptophol
-
structural analogue to tryptamine
-
-
?
acetyl-CoA + tyramine
CoA + ?
8% of the activity with 2-phenylethylamine
-
-
?
arachidonoyl-CoA + octopamine
CoA + N-arachidonoyloctopamine
-
-
-
?
palmitoyl-CoA + octopamine
CoA + N-palmitoyloctopamine
-
-
-
?
acetyl-CoA + 2-(2,3-dichlorophenyl)-ethylamine
CoA + N-acetyl-2-(2,3-dichlorophenyl)-ethylamine
78% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(2,3-dichlorophenyl)-ethylamine
CoA + N-acetyl-2-(2,3-dichlorophenyl)-ethylamine
-
84% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(2-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(2-chlorophenyl)-ethylamine
130% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(2-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(2-chlorophenyl)-ethylamine
-
102% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine
7% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine
-
64% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3,4-dimethoxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dimethoxyphenyl)-ethylamine
4.4% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3,4-dimethoxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dimethoxyphenyl)-ethylamine
-
15% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(3-chlorophenyl)-ethylamine
67% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(3-chlorophenyl)-ethylamine
-
110% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(3-fluorophenyl)-ethylamine
65% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(3-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(3-fluorophenyl)-ethylamine
-
93% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(4-bromophenyl)-ethylamine
CoA + N-acetyl-2-(4-bromophenyl)-ethylamine
48% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(4-bromophenyl)-ethylamine
CoA + N-acetyl-2-(4-bromophenyl)-ethylamine
-
87% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(4-chlorophenyl)ethylamine
CoA + N-acetyl-2-(4-chlorophenyl)ethylamine
68% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(4-chlorophenyl)ethylamine
CoA + N-acetyl-2-(4-chlorophenyl)ethylamine
-
91% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(4-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(4-fluorophenyl)-ethylamine
116% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(4-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(4-fluorophenyl)-ethylamine
-
60% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(p-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(p-fluorophenyl)-ethylamine
56% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(p-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(p-fluorophenyl)-ethylamine
-
as active as with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(p-nitrophenyl)-ethylamine
CoA + N-acetyl-2-(p-nitrophenyl)-ethylamine
9% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(p-nitrophenyl)-ethylamine
CoA + N-acetyl-2-(p-nitrophenyl)-ethylamine
-
53% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(p-tolyl)-ethylamine
CoA + N-acetyl-2-(p-tolyl)-ethylamine
60% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-(p-tolyl)-ethylamine
CoA + N-acetyl-2-(p-tolyl)-ethylamine
-
87% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-methoxyphenylethylamine
CoA + N-acetyl-2-methoxyphenylethylamine
52% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-methoxyphenylethylamine
CoA + N-acetyl-2-methoxyphenylethylamine
-
97% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 2-phenylethylamine
CoA + N-acetyl-2-phenylethylamine
-
-
-
?
acetyl-CoA + 2-phenylethylamine
CoA + N-acetyl-2-phenylethylamine
-
-
-
-
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonyl fluoride
CoA + ?
8% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonyl fluoride
CoA + ?
-
7.4% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 4-methoxyphenylethylamine
CoA + N-acetyl-4-methoxyphenylethylamine
11% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 4-methoxyphenylethylamine
CoA + N-acetyl-4-methoxyphenylethylamine
-
10% of the activity with 2-phenylethylamine
-
-
?
acetyl-CoA + 5-hydroxytryptamine
CoA + N-acetyl-5-hydroxytryptamine
-
-
-
-
?
acetyl-CoA + 5-hydroxytryptamine
CoA + N-acetyl-5-hydroxytryptamine
-
-
-
-
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
-
-
-
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
-
-
-
?
acetyl-CoA + 6-fluorotryptamine
CoA + N-acetyl-6-fluorotryptamine
-
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
also substrate: phenylethylamine derivatives without a beta-hydroxy group
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
i.e. 5-hydroxytryptamine
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
rate-limiting in melatonin, i.e. N-acetyl-5-methoxytryptamine synthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
key enzyme of circadian rhythm of melatonin synthesis
-
-
-
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
rate-limiting in melatonin synthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
the enzyme catalyzes the first step in melatonin biosynthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
i.e. 5-hydroxytryptamine
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
i.e. 5-hydroxytryptamine
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
initial reaction in melatonin synthesis from serotonin
-
-
-
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
penultimate enzyme in melatonin pathway
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
penultimate step in melatonin biosynthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
reaction mechanism involving Pro64 that plays a critical role in structure and catalysis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
i.e. 5-hydroxytryptamine
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
i.e. 5-hydroxytryptamine
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
i.e. 5-hydroxytryptamine
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
initial reaction in melatonin synthesis from serotonin
-
-
-
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
first step in melatonin biosynthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
AANAT2 acetylates serotonin about 10times faster than AANAT1
-
-
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
-
-
-
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
10% of the activity with 2-phenylethylamine
-
-
?
additional information
?
-
-
aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
-
-
-
additional information
?
-
aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
-
-
-
additional information
?
-
-
substrate specificity, aaNAT1 and aaNAT2 show a broad substrate specificity and their affinity and catalytic efficiency to each of the seven arylalkylamines tested. The affinity between aaNAT1 and aaNAT2 to most of the arylalkylamines is similar except that aaNAT2 has less affinity than aaNAT1 to norepinephrine. Also aaNAT1 is more efficient in catalyzing all the tested substrates than that of aaNAT2
-
-
-
additional information
?
-
-
ordered sequential mechanism, with acetyl-CoA binding first followed by histamine to generate an AANATL7-acetyl-CoA-histamine ternary complex prior to catalysis. An ionizable group with a pKa of 7.1 is assigned to Glu-26 as a general base and a second with a pKa of 9.5 is assigned to the protonation of the thiolate of the coenzyme A product
-
-
-
additional information
?
-
-
enzyme activity in cultured cells is suppressed by light, as it is in vivo. The ability to express circadian regulation of the enzyme activity is an intrinsic property of retinal cells that can develop in vitro
-
-
-
additional information
?
-
-
further substrates: selected synthetic amines
-
-
-
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis
-
-
-
additional information
?
-
no activity with 2-(4-aminophenyl)-ethylamine, 3,4-(dibenzyloxy)phenethylamine, 5-hydroxydopamine, 4-(2-aminoethyl)-benzenesulfonamide or 2-(p-chlorophenoxy)-2-methylpropionic acid
-
-
-
additional information
?
-
-
enzyme light and diurnal regulation involves phosphorylation on key AANAT Ser and Thr residues, which results in 14-3-3 protein recruitment and changes in catalytic activity and protein stability
-
-
-
additional information
?
-
the enzyme catalyzes the limiting step for melatonin synthesis
-
-
-
additional information
?
-
-
arylamines, such as aniline or p-phenetidine are very poor substrates
-
-
-
additional information
?
-
-
arylamines, such as aniline or p-phenetidine are very poor substrates
-
-
-
additional information
?
-
-
no activity with 2-(4-aminophenyl)-ethylamine, 3,4-(dibenzyloxy)phenethylamine or 2-(p-chlorophenoxy)-2-methylpropionic acid
-
-
-
additional information
?
-
-
NAT could be a clock-controlled gene functioning as an output regulator of the circadian clock
-
-
-
additional information
?
-
-
no substrates are phenylethanolamine derivatives with a beta-hydroxy group
-
-
-
additional information
?
-
-
arylamines, such as aniline or p-phenetidine are very poor substrates
-
-
-
additional information
?
-
-
arylamines, such as aniline or p-phenetidine are very poor substrates
-
-
-
additional information
?
-
-
overexpression of inducible cAMP early repressor can suppress the norepinephrine induction of aa-nat
-
-
-
additional information
?
-
AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
-
-
-
additional information
?
-
AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
-
-
-
additional information
?
-
-
AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
-
-
-
additional information
?
-
AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
-
-
-
additional information
?
-
AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
-
-
-
additional information
?
-
-
AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
-
-
-
additional information
?
-
insignificant activity in presence of phenylethylamine or tyramine
-
-
-
additional information
?
-
insignificant activity in presence of phenylethylamine or tyramine
-
-
-
additional information
?
-
-
insignificant activity in presence of phenylethylamine or tyramine
-
-
-
additional information
?
-
-
AANAT is a key regulatory enzyme in the melatonin biosynthetic pathway
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
Q16KL9
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
-
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
-
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
rate-limiting in melatonin, i.e. N-acetyl-5-methoxytryptamine synthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
key enzyme of circadian rhythm of melatonin synthesis
-
-
-
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
rate-limiting in melatonin synthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
the enzyme catalyzes the first step in melatonin biosynthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
initial reaction in melatonin synthesis from serotonin
-
-
-
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
penultimate enzyme in melatonin pathway
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
penultimate step in melatonin biosynthesis
-
-
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
initial reaction in melatonin synthesis from serotonin
-
-
-
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
first step in melatonin biosynthesis
-
-
?
additional information
?
-
-
aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
-
-
-
additional information
?
-
Q16KL9
aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
-
-
-
additional information
?
-
-
enzyme activity in cultured cells is suppressed by light, as it is in vivo. The ability to express circadian regulation of the enzyme activity is an intrinsic property of retinal cells that can develop in vitro
-
-
-
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis
-
-
-
additional information
?
-
-
enzyme light and diurnal regulation involves phosphorylation on key AANAT Ser and Thr residues, which results in 14-3-3 protein recruitment and changes in catalytic activity and protein stability
-
-
-
additional information
?
-
Q9PT39
the enzyme catalyzes the limiting step for melatonin synthesis
-
-
-
additional information
?
-
-
NAT could be a clock-controlled gene functioning as an output regulator of the circadian clock
-
-
-
additional information
?
-
-
overexpression of inducible cAMP early repressor can suppress the norepinephrine induction of aa-nat
-
-
-
additional information
?
-
Q68SL6
AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
-
-
-
additional information
?
-
Q68SL7
AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
-
-
-
additional information
?
-
-
AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
-
-
-
additional information
?
-
Q68SL6
AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
-
-
-
additional information
?
-
Q68SL7
AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
-
-
-
additional information
?
-
-
AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
-
-
-
additional information
?
-
-
AANAT is a key regulatory enzyme in the melatonin biosynthetic pathway
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activation by salts as a function of ionic strength
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9-carboxy-11-nor-delta-9-tetrahydrocannabinol
-
significantly reduces norepinephrine-induced arylalkylamine N-acetyltransferase activity
cannabidiol
-
significantly reduces norepinephrine-induced arylalkylamine N-acetyltransferase activity
cannabinoid
-
cannabinoids inhibit AANAT activity and attenuate melatonin biosynthesis through intracellular actions without involvement of classical cannabinoid receptor-dependent signaling cascades
cannabinol
-
significantly reduces norepinephrine-induced arylalkylamine N-acetyltransferase activity
CoA-S-N-acetyl-7-hydroxynaphthylethylamine
-
fluorescent variant of CoA-T, a bisubstrate inhibitor, synthesis and enzyme binding structure, molecular modelling, overview
CoA-S-N-acetyltryptamine
total inhibition of N-acetyldopamine synthesis in presence of acetyl coenzyme-A and dopamine occurs in the presence of CoA-S-N-acetyltryptamine in liver
methyl 3-[2-[(bromoacetyl)amino]ethyl]-1-benzothiophene-5-carboxylate
-
IC50: 0.00225 mM
N-[2-(7-ethyl-1,2,3,4-tetrahydronapht-1-yl)ethyl]iodooacetamide
-
IC50: above 0.1 mM
N-[2-(7-methoxy-3-(3-trifluoromethylphenyl)-napht-1-yl)ethyl]iodoacetamide
-
IC50: 0.045 mM
tryptamine-coenzyme A
-
a bisubstrate inhibitor, enzyme binding structure, molecular modelling, overview
UV light
-
NAT activity and melatonin content are suppressed by blue light of 450 nm wavelength, no effects of red light at 650 nm.UV radiation has intensity-dependent dual effects on the NAT activity and melatonin content: it is supressing at low intensity and activating at high intensity irradiation, overview
-
additional information
-
both white and blue light pulses significantly inhibit AA-NAT activity at zeitgeber time ZT18, detailed overview
-
additional information
both white and blue light pulses significantly inhibit AA-NAT activity at zeitgeber time ZT18, detailed overview
-
additional information
no inhibition by serotonin or tryptamin above 1 mM. No inhibition by melatonin
-
additional information
-
no inhibition by serotonin or tryptamin above 1 mM. No inhibition by melatonin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14-3-3 protein
-
14-3-3zeta, interaction with the phosphorylated enzyme activates activity, binding analysis, overview
-
4beta-phorbol 12-myristate 13-acetate
-
stimulates activity on a posttranscriptional level in a cAMP-independent manner
leptin
-
increases enzyme activity only in fed fish not in fasted fish, independently of the seasons
-
UV light
-
NAT activity and melatonin content are suppressed by blue light of 450 nm wavelength, no effects of red light at 650 nm.UV radiation has intensity-dependent dual effects on the NAT activity and melatonin content: it is supressing at low intensity and activating at high intensity irradiation, overview
-
additional information
-
the enzyme is activated by Ser and Thr phosphorylations, e.g. AANAT Thr31 phosphorylation on its own can enhance catalytic efficiency up to 7fold
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
Arachidonoyl-CoA
pH 8.0, temperature not specified in the publication
0.0036
oleoyl-CoA
pH 8.0, temperature not specified in the publication
0.0099
palmitoyl-CoA
pH 8.0, temperature not specified in the publication
0.006
stearoyl-CoA
pH 8.0, temperature not specified in the publication
0.0061
acetyl-CoA
pH 8.0, temperature not specified in the publication
0.029
acetyl-CoA
-
mutant T167A/S171A, pH 8.0, 22°C; wild-type, pH 8.0, 22°C
0.0018
Butanoyl-CoA
pH 8.0, temperature not specified in the publication
4
tryptamine
-
above, pH 6.8, 37°C, recombinant mutants P64A, P64G, P64W, and recombinant truncation mutants
additional information
additional information
-
formation and cleavage of a disulfide bond produce active/inactive states of enzyme
-
additional information
additional information
-
exposing chickens to light in the middle of the night increased the apparent Km of AANAT for tryptamine by about 10fold. The Km began to increase within 5 min of exposure to light and reached a maximum at about 30 min
-
additional information
additional information
-
kinetics of recombinant partially phosphorylated wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes, substrate tryptamine, overview
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
-
AANAT2 kinetic constants as a function of temperature, overview
-
additional information
additional information
-
AANAT2 kinetics in relation to temperature, overview
-
additional information
additional information
-
AANAT2 kinetics in relation to temperature, overview
-
additional information
additional information
-
AANAT2 kinetic constants as a function of temperature, overview
-
additional information
additional information
-
AANAT2 kinetic constants as a function of temperature, overview
-
additional information
additional information
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b; both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
additional information
additional information
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b; both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
additional information
additional information
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b; both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
Arachidonoyl-CoA
pH 8.0, temperature not specified in the publication
0.075
oleoyl-CoA
pH 8.0, temperature not specified in the publication
0.16
palmitoyl-CoA
pH 8.0, temperature not specified in the publication
0.059
stearoyl-CoA
pH 8.0, temperature not specified in the publication
1.3
acetyl-CoA
pH 8.0, temperature not specified in the publication
0.53
Butanoyl-CoA
pH 8.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
Arachidonoyl-CoA
pH 8.0, temperature not specified in the publication
21
oleoyl-CoA
pH 8.0, temperature not specified in the publication
16
palmitoyl-CoA
pH 8.0, temperature not specified in the publication
9.8
stearoyl-CoA
pH 8.0, temperature not specified in the publication
220
acetyl-CoA
pH 8.0, temperature not specified in the publication
290
Butanoyl-CoA
pH 8.0, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00039
2-bromo-N-[2-(5-fluoro-1-benzothien-3-yl)ethyl]acetamide
Homo sapiens;
-
IC50: 0.00039 mM
0.00225
methyl 3-[2-[(bromoacetyl)amino]ethyl]-1-benzothiophene-5-carboxylate
Homo sapiens;
-
IC50: 0.00225 mM
0.0087
N-[2-(2-benzyl-5-methoxy-benzofuran-3-yl)ethyl]iodoacetamide
Homo sapiens;
-
IC50: 0.0087 mM
0.001
N-[2-(2-phenyl-benzo [b]thiophen-3-yl)ethyl]bromoacetamide
Homo sapiens;
-
IC50: 0.001 mM
0.0006
N-[2-(3-ethyl-7-methoxy-napht-1-yl)ethyl]iodoacetamide
Homo sapiens;
-
IC50: 0.0006 mM
0.00378
N-[2-(5-bromo-benzo[b]thiophen-3-yl)ethyl]bromoacetamide
Homo sapiens;
-
IC50: 0.00378 mM
0.00018
N-[2-(5-chloro-benzo[b]thiophen-3-yl)ethyl]bromoacetamide
Homo sapiens;
-
IC50: 0.00018 mM
0.00071
N-[2-(5-ethyl-benzo[b]thiophen-3-yl)ethyl]bromoacetamide
Homo sapiens;
-
IC50: 0.00071 mM
0.00018
N-[2-(5-hydroxy-benzo[b]thiophen-3-yl)ethyl]bromoacetamide
Homo sapiens;
-
IC50: 0.00018 mM
0.1
N-[2-(7-ethyl-1,2,3,4-tetrahydronapht-1-yl)ethyl]iodooacetamide
Homo sapiens;
-
IC50: above 0.1 mM
0.045
N-[2-(7-methoxy-3-(3-trifluoromethylphenyl)-napht-1-yl)ethyl]iodoacetamide
Homo sapiens;
-
IC50: 0.045 mM
0.1
N-[2-(7-methoxy-8-propenyl-napht-1-yl)ethyl]-iodoacetamide
Homo sapiens;
-
IC50: above 0.1 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000027
-
enzyme activity on pineal in pineal gland from quiescent phase, pH 6.5, 25°C
0.000036
-
enzyme activity on pineal in pineal gland from progressive phase, pH 6.5, 25°C
0.000039
-
enzyme activity on pineal in pineal gland from breeding phase, pH 6.5, 25°C
0.000043
-
enzyme activity on pineal in pineal gland from regressive phase, pH 6.5, 25°C
additional information
additional information
-
enzyme activities of recombinant wild-type and mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
7.5
9.5
-
two pH optima, pH 6.0 and pH 9.5, which change during oocyte maturation
6
-
two pH optima, pH 6.0 and pH 9.5, which change during oocyte maturation
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
pH 6.5: about 30% of maximal activity, pH 8.0: about 50% of maximal activity
7 - 8
pH 7.0: abut 40% of maximal activity, pH 8.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
37
additional information
-
pineal AANAT responds to temperature in a species-specific manner
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
0°C: about 55% of maximal activity, 47°C: about 50% of maximal activity
20 - 47
20°C: about 40% of maximal activity, 47°C: about 35% of maximal activity
additional information
additional information
-
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview
additional information
-
AANAT2 primary to tertiary structures and kinetic constants as a function of temperature, overview
additional information
-
AANAT2 primary to tertiary structures and kinetic constants as a function of temperature, overview
additional information
-
AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview
additional information
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AANAT2 primary to tertiary structures and kinetics in relation to temperature, overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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female. The left gland contains higher activity than the right gland
strongly expressed in the head, fat body, midgut, and integument tubules of 5th instar larvae
esophagus, stomach, pyloric ceca, foregut, midgut, hindgut. AANAT2 is expressed only in the muscular layer of all segments. No significant differences are obtained among the different segments evaluated
in foregut AANAT activity shows a daily rhythm while in hindgut significant but not rhythmic levels of AANAT activity are found. The active isoform in gut is AANAT1
A0A0K1H4R1;, B9TU30;, B9TU31;
isoforms Aanat1a and Aanat1b display a wide and distinct distribution in the nervous system and peripheral tissues; isoforms Aanat1a and Aanat1b display a wide and distinct distribution in the nervous system and peripheral tissues
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photoreceptor cells, ependymal cells of the 3rd ventricle and discrete cells of the suprachiasmatic area. Expression of AANAT2 and absence of AANAT2
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mainly pars tuberalis, much less than in pineal gland, probably different regulation
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AANAT-specific immunoreactivity is observed in the nuclei of spinal neurons, and is significantly increased in aged dog spinal neurons compared to young adult spinal neurons. Melatonin receptor type 1B-specific immunoreactivity is found in the cytoplasm of spinal neurons, and is predominantly increased in the margin of the neuron cytoplasm in aged spinal cord compared to that in the young adult dogs
additional information
the enzymatic activity is higher in adult than in pupal brain. No difference is observed between day and night in the pupal brain and adult brain
strongly expressed in the head, fat body, midgut, and integument tubules of 5th instar larvae
strongly expressed in the head, fat body, midgut, and integument tubules of 5th instar larvae
in liver significant but not rhythmic levels of AANAT activity are found