2.3.1.87: aralkylamine N-acetyltransferase
This is an abbreviated version!
For detailed information about aralkylamine N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.87
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2.3.1.87
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melatonin
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pineal
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rhythm
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circadian
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clock
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retina
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night
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nocturnal
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norepinephrine
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hiomt
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pinealocytes
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arylalkylamine-n-acetyltransferase
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hydroxyindole-o-methyltransferase
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photoreceptors
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oscillator
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n-acetylserotonin
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diurnal
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suprachiasmatic
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photoperiodic
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snats
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light-dark
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sodium-coupled
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adrenergic
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tryptamine
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entrain
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photoreceptive
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synthesis
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n-acetyl-5-methoxytryptamine
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gcn5-related
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photic
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zeitgeber
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clockwork
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day-night
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octopamine
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night-time
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clock-controlled
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medicine
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analysis
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ne-stimulated
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hydroxyindole
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meaib
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melatoninergic
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rhythm-generating
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extrapineal
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slc38a2
- 2.3.1.87
- melatonin
-
pineal
- rhythm
-
circadian
- clock
- retina
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night
-
nocturnal
- norepinephrine
- hiomt
- pinealocytes
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arylalkylamine-n-acetyltransferase
- hydroxyindole-o-methyltransferase
- photoreceptors
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oscillator
- n-acetylserotonin
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diurnal
-
suprachiasmatic
-
photoperiodic
-
snats
-
light-dark
-
sodium-coupled
-
adrenergic
- tryptamine
-
entrain
-
photoreceptive
- synthesis
- n-acetyl-5-methoxytryptamine
-
gcn5-related
-
photic
-
zeitgeber
-
clockwork
-
day-night
- octopamine
-
night-time
-
clock-controlled
- medicine
- analysis
-
ne-stimulated
-
hydroxyindole
-
meaib
-
melatoninergic
-
rhythm-generating
-
extrapineal
-
slc38a2
Reaction
Synonyms
AA-NAT, AANAT, AANAT1, AANAT2, AANAT3, AANATL7, AATNATL2, acetyl-CoA:aralkylamine N-acetyltransferase, acetyltransferase, arylalkylamine N-, arylalkylamine N-acetyltransferase, arylalkylamine N-acetyltransferase 1, arylalkylamine N-acetyltransferase 1a, arylalkylamine N-acetyltransferase 1b, arylalkylamine N-acetyltransferase 2, arylalkylamine N-acetyltransferase like 7, arylalkylamine N-acetyltransferase-2, Bm-iAANAT, Eis, hAANAT, More, MSMEG_3513, N-acetyltransferase, NAT, oAANAT, PA4534, PaaNAT, Rv2416c, serotonin acetylase, serotonin acetyltransferase, serotonin N-acetyltransferase, serotonin-N-acetyltransferase, SNA, SNAT, SNAT1, SNAT2
ECTree
2.3.1.87 aralkylamine N-acetyltransferaseAdvanced search results
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results (General Information
General Information on EC 2.3.1.87 - aralkylamine N-acetyltransferase
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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
metabolism
physiological function
additional information
evolution
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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
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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
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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
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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
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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
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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
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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
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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
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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
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the enzyme catalyzes the rate-limiting step in melatonin synthesis
metabolism
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the enzyme catalyzes the rate-limiting step in melatonin synthesis, melatonin biosynthesis pathway overview
metabolism
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arylalkylamine N-acetyltransferase is the rate-limiting enzyme of the melatonin biosynthesis pathway
metabolism
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serotonin N-acetyltransferase is a rate-limiting enzyme in melatonin biosynthesis in vertebrates
metabolism
N-terminally acetylated Ac-AANAT is degraded through the recognition of its N-terminally acetylated N-terminal Met residue by the Ac/N-end rule pathway, whereas the non-N-terminally acetylated AANAT is targeted by the Arg/N-end rule pathway, which recognizes the unacetylated N-terminal Met-Leu sequence of rat AANAT. Degradation of Lys8Arg mutants of rat AANAT is mediated by polyubiquitylation of its Lys residue(s)
metabolism
the N-terminal sequence of human AANAT differs from that of rodent AANATs. The human enzyme is longer-lived than its rat counterpart and appears to be refractory to degradation by the N-end rule pathway
physiological function
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AANAT is a key circadian rhythm enzyme that drives the nocturnal production of melatonin in the pineal
physiological function
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Aanat2 is the main enzyme responsible of the plasma nocturnal melatonin increase in the fish
physiological function
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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
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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
aaNATs are involved in sclerotization and neurotransmitter inactivation in insects
physiological function
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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
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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
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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
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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
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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
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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
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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-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
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
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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
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
physiological function
isoform AANAT1 is an important enzyme in the regulation of dopamine and N-acetyldopamine content in liver
physiological function
isoform Aanat2 is a pineal enzyme involved in melatonin production
physiological function
isoform AANATL2 has a role in the biosynthetic formation of long-chain N-acylserotonins and N-acydopamines
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
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a knockout mutant exhibits delayed flowering. Melatonin levels are 50% lower in flowers of the mutant than in those of the wild-type, but the melatonin levels of leaves do not differ
physiological function
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a significant negative correlation exists between plasma levels of the thyroid hormones T3 and T4 and AANAT activity. A direct relationship exists between water temperature/daylength and plasma levels of thyroid hormones, and an inverse relationship between water temperature/daylength and AANAT activity. The acrophase (peak) of the circadian rhythm of both T3 and T4 occurs around midday, while the acrophase of AANAT activity rhythm is recorded during midnight
physiological function
AANAT levels and melatonin synthesis increase after TRPV4 channel stimulation in ciliary body epithelium
physiological function
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CoA and acetyl-CoA alter the conformation of the substrate binding site of arylalkylamine N-acetyltransferase to facilitate interaction with acceptor substrates. It is the presence of the acetyl group within the catalytic funnel that triggers high affinity binding. Acetyl group occupancy is relayed through a conserved salt bridge between the P-loop and the acceptor binding site, and is manifested as differential dynamics in the CoA and acetyl-CoA-bound states
physiological function
loss of function of AANAT1 caused by RNAi has no effect on larval and pupal development. The tanning of pupal setae, gin traps and urogomphi proceeds normally. About 70% of the resulting adults exhibit a roughened exoskeletal surface, separated elytra and improperly folded hindwings. The body wall, elytra and veins of the hindwing of the mature adults are significantly darker than those of control insects probably due to the accumulation of dopamine melanin
physiological function
suppression of both isoforms SNAT1 and SNAT2 leads to retarded seedling growths in conjunction with severe decreases in melatonin compared to wild-types and single-suppression rice plants. The laminar angle is decreased in the SNAT1/SNAT2 suppression rice compared to that of the wild-types and SNAT1 suppression, but is comparable to that of SNAT2 suppression strain. The reduced germination speed in the SNAT1/SNAT2 suppression strain is comparable to that of SNAT2 suppression lines. The SNAT1 suppression strain is the most severely deteriorated, followed by SNAT1/SNAT2 suppression and SNAT2 suppression strains
physiological function
transgenic rice plants overexpressing rice SNAT1 do not show enhanced seedling growth. SNAT1-overexpressing rice plants show significant resistance to cadmium and senescence stresses relative to wild-type controls. Melatonin synthesis in rice seedlings is not induced by selenium and SNAT1 transgenic rice plants do not show tolerance to selenium. T2 homozygous SNAT1 transgenic rice plants exhibit increased grain yield due to increased panicle number per plant under paddy field conditions
physiological function
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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
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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
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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
additional information
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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
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