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Information on EC 2.1.1.4 - acetylserotonin O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.4
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.4 acetylserotonin O-methyltransferase
IUBMB Comments
Some other hydroxyindoles also act as acceptor, but more slowly.
The enzyme appears in viruses and cellular organisms
- 2.1.1.4
- melatonin
-
pineal
- n-acetyltransferase
-
rhythm
- retina
-
circadian
-
nocturnal
-
night
- arylalkylamine
- pinealocytes
-
diurnal
- photoreceptors
-
photoperiodic
-
melatoninergic
-
harderian
-
melatonin-synthesizing
-
daytime
-
nighttime
- 5-hydroxytryptophan
- aa-nat
-
arylalkylamine-n-acetyltransferase
- 5-methoxytryptophan
- 5-methoxytryptamine
- 5-hydroxyindole
- n-acetyl-5-methoxytryptamine
-
pinealectomized
- serotonin-n-acetyltransferase
-
5-hydroxyindoleacetic
- 5-methoxyindoles
- analysis
-
light:dark
- synthesis
-
ganglionectomy
-
extrapineal
Reaction Schemes
showSynonyms
hiomt, hydroxyindole-o-methyltransferase, hydroxyindole o-methyltransferase, n-acetylserotonin methyltransferase, n-acetylserotonin o-methyltransferase, acetylserotonin o-methyltransferase, hydroxyindole-o-methyl transferase, acetylserotonin methyltransferase, asmt2, asmt1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylserotonin methyltransferase
-
-
-
-
ASMT
ASMT1
ASMT2
ASMT3
COMT
COMT1
HIOMT
hydroxyindole methyltransferase
-
-
-
-
hydroxyindole O-methyltransferase
hydroxyindole-O-methyl transferase
-
-
-
-
hydroxyindole-O-methyltransferase
methyltransferase, acetylserotonin
-
-
-
-
N-acetylserotonin methyltransferase
N-acetylserotonin O-methyltransferase
ASMT
-
-
-
-
HIOMT
-
-
-
-
hydroxyindole O-methyltransferase
-
-
-
-
N-acetylserotonin O-methyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
reaction sequence is ordered bi-bi type
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
reaction sequence is ordered bi-bi type
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
reaction sequence is ordered bi-bi type
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
reaction sequence is ordered bi-bi type
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
reaction sequence is ordered bi-bi type
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
addition of S-adenosyl-L-methionine occuring first followed by N-acetylserotonin
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
addition of S-adenosyl-L-methionine occuring first followed by N-acetylserotonin
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
addition of S-adenosyl-L-methionine occuring first followed by N-acetylserotonin
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
addition of S-adenosyl-L-methionine occuring first followed by N-acetylserotonin
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
addition of S-adenosyl-L-methionine occuring first followed by N-acetylserotonin
-
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
modeling of the catalytic mechanism
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
O-methylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
serotonin and melatonin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:N-acetylserotonin O-methyltransferase
Some other hydroxyindoles also act as acceptor, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
9029-77-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxy-N-acetyltryptamine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-4-methoxytryptamine
-
Substrates: 8% of the activity with N-acetylserotonin
Products: -
Products: -
?
5-hydroxyindoleacetic acid + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + 5-methoxyindoleacetic acid
-
Substrates: 12% of the activity with N-acetylserotonin
Products: -
Products: -
?
bufotenine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N,N-dimethyl-5-hydroxytryptamine
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
N-methylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-methyl-5-methoxytryptamine
-
Substrates: 9% of the activity with N-acetylserotonin
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
bufotenine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N,N-dimethyl-5-hydroxytryptamine
-
Substrates: -
Products: -
Products: -
?
bufotenine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N,N-dimethyl-5-hydroxytryptamine
-
Substrates: 14% of the activity with N-acetylserotonin
Products: -
Products: -
?
bufotenine + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N,N-dimethyl-5-hydroxytryptamine
-
Substrates: -
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: the enzyme is involved in melatonin biosynthesis in egg yolk, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
Frog
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + serotonin
S-adenosyl-L-homocysteine + 5-methoxytryptamine
Substrates: enzyme AtASMT also O-methylates serotonin to produce 5-methoxytryptamine
Products: -
Products: -
?
S-adenosyl-L-methionine + serotonin
S-adenosyl-L-homocysteine + 5-methoxytryptamine
Substrates: enzyme AtASMT also O-methylates serotonin to produce 5-methoxytryptamine
Products: -
Products: -
?
serotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + 5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
serotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + 5-methoxytryptamine
-
Substrates: 7% of the activity with N-acetylserotonin
Products: -
Products: -
?
serotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + 5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the AtASMT protein catalyzes the conversion of N-acetylserotonin to melatonin and serotonin to 5-methoxytryptamine, respectively. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
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additional information
?
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Substrates: the AtASMT protein catalyzes the conversion of N-acetylserotonin to melatonin and serotonin to 5-methoxytryptamine, respectively. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
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additional information
?
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Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. COMT is a multifunctional enzyme methylating a diverse array of substrates, including phenylpropanoids, flavonoids, and arylalkylamines
Products: -
Products: -
?
additional information
?
-
-
Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. COMT is a multifunctional enzyme methylating a diverse array of substrates, including phenylpropanoids, flavonoids, and arylalkylamines
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Products: -
?
additional information
?
-
Substrates: caffeic acid is no substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: caffeic acid is no substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the AtASMT protein catalyzes the conversion of N-acetylserotonin to melatonin and serotonin to 5-methoxytryptamine, respectively. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: caffeic acid is no substrate
Products: -
Products: -
?
additional information
?
-
Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. COMT is a multifunctional enzyme methylating a diverse array of substrates, including phenylpropanoids, flavonoids, and arylalkylamines
Products: -
Products: -
?
additional information
?
-
-
Substrates: absolute requirement for S-adenosylmethionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: bovine enzyme has high specificity towards N-acetylserotonin, chicken enzyme methylates N-acetylserotonin and to some extent serotonin and bufotenine
Products: -
Products: -
?
additional information
?
-
Substrates: COMT exhibits a notably higher affinity for caffeic acid (reaction of EC 2.1.1.68) compared to N-acetylserotonin
Products: -
Products: -
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additional information
?
-
-
Substrates: absolute requirement for S-adenosylmethionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: bovine enzyme has high specificity towards N-acetylserotonin, chicken enzyme methylates N-acetylserotonin and to some extent serotonin and bufotenine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also catalyzes the conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: absolute requirement for S-adenosylmethionine
Products: -
Products: -
?
additional information
?
-
Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. The ASMT activity (Vmax/Km) of OsCOMT is 609fold higher than that of rice ASMT1
Products: -
Products: -
?
additional information
?
-
-
Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. The ASMT activity (Vmax/Km) of OsCOMT is 609fold higher than that of rice ASMT1
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is controlled by the endogenous clock
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additional information
?
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Substrates: in pineal glands isolated in the morning 4 h magnetic field exposure changes melatonin release by affecting the signal transduction pathway leading from the norepinephrine receptor to N-acetyltransferase and hydroxyindole-O-methyltransferase and not via a direct effect at the enzyme levels
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additional information
?
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Substrates: in pineal glands isolated in the morning 4 h magnetic field exposure changes melatonin release by affecting the signal transduction pathway leading from the norepinephrine receptor to N-acetyltransferase and hydroxyindole-O-methyltransferase and not via a direct effect at the enzyme levels
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
Substrates: formation of the hormone melatonin
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: the enzyme is involved in melatonin biosynthesis in egg yolk, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
Products: -
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S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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Substrates: -
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S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
Substrates: -
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S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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Substrates: -
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S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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Substrates: -
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S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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S-adenosyl-L-methionine + serotonin
S-adenosyl-L-homocysteine + 5-methoxytryptamine
Substrates: enzyme AtASMT also O-methylates serotonin to produce 5-methoxytryptamine
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S-adenosyl-L-methionine + serotonin
S-adenosyl-L-homocysteine + 5-methoxytryptamine
Substrates: enzyme AtASMT also O-methylates serotonin to produce 5-methoxytryptamine
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Substrates: the AtASMT protein catalyzes the conversion of N-acetylserotonin to melatonin and serotonin to 5-methoxytryptamine, respectively. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
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additional information
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Substrates: the AtASMT protein catalyzes the conversion of N-acetylserotonin to melatonin and serotonin to 5-methoxytryptamine, respectively. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
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Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. COMT is a multifunctional enzyme methylating a diverse array of substrates, including phenylpropanoids, flavonoids, and arylalkylamines
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additional information
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Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. COMT is a multifunctional enzyme methylating a diverse array of substrates, including phenylpropanoids, flavonoids, and arylalkylamines
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additional information
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Substrates: the AtASMT protein catalyzes the conversion of N-acetylserotonin to melatonin and serotonin to 5-methoxytryptamine, respectively. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
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additional information
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Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. COMT is a multifunctional enzyme methylating a diverse array of substrates, including phenylpropanoids, flavonoids, and arylalkylamines
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additional information
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Substrates: the enzyme also catalyzes the conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate
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additional information
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Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. The ASMT activity (Vmax/Km) of OsCOMT is 609fold higher than that of rice ASMT1
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additional information
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Substrates: caffeic acid O-methyltransferase (COMT), EC 2.1.1.68, methylates N-acetylserotonin into melatonin, it has N-acetylserotonin O-methyltransferase (ASMT) activity. The ASMT activity (Vmax/Km) of OsCOMT is 609fold higher than that of rice ASMT1
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Substrates: in pineal glands isolated in the morning 4 h magnetic field exposure changes melatonin release by affecting the signal transduction pathway leading from the norepinephrine receptor to N-acetyltransferase and hydroxyindole-O-methyltransferase and not via a direct effect at the enzyme levels
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Substrates: in pineal glands isolated in the morning 4 h magnetic field exposure changes melatonin release by affecting the signal transduction pathway leading from the norepinephrine receptor to N-acetyltransferase and hydroxyindole-O-methyltransferase and not via a direct effect at the enzyme levels
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ASMT-specific activity is not altered by the addition of EDTA or the divalent cation Mg2+, suggesting that Oryza sativa ASMT is a cation-independent O-methyltransferase
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
caffeic acid
in vitro N-acetylserotonin methyltransferase activity is significantly and competitively inhibited by caffeic acid, a substrate of the caffeic acid O-methyltransferase, 73% inhibition at 0.01 mM, 93% at 0.1 mM
cysteamine
-
rat enzyme inhibited to 50% at 0.128 mM, bovine and ovine enzyme not
fisetin
0.1 mM, strong inhibition of N-acetylserotonin methyltransferase activity
kaempferol
0.1 mM, strong inhibition of N-acetylserotonin methyltransferase activity
L-glutamate
-
inhibition is reversible, dose-dependent, no inhibition of mRNA expression
luteolin
0.1 mM, strong inhibition of N-acetylserotonin methyltransferase activity
morin
0.1 mM, strong inhibition of N-acetylserotonin methyltransferase activity
myricetin
0.1 mM, strong inhibition of N-acetylserotonin methyltransferase activity
quercetin
in vitro N-acetylserotonin methyltransferase activity is significantly and competitively inhibited by quercetin, a substrate of the caffeic acid O-methyltransferase, in vivo production of melatonin is significantly inhibited by quercetin in 4-week-old detached rice leaves, 97% inhibition at 0.01 mM, complete inhibition at over 0.05 mM
quercetin
0.1 mM, strong inhibition of N-acetylserotonin methyltransferase activity
additional information
-
various amine compounds, including tyramine, tryptamine, N-acetyltryptamine, and 5-methoxytryptamine show no or poor inhibition of the enzyme. The enzyme does not show substrate inhibition at high N-acetylserotonin concentrations
-
additional information
all of the flavonoids tested greatly inhibit the ASMT activity of COMT, and thus the melatonin biosynthetic activity, with the exception of catechin
-
additional information
-
not inhibitory: (2S,2'R,3'R)-2-(2',3'-dicarboxycyclopropyl)glycine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
retinoic acid stereoisomers induce an increase in activity and mRNA level
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
ASMT Regulates Tumor Metastasis Through the Circadian Clock System in Triple-Negative Breast Cancer.
Breast Neoplasms
Cytoguardin: A Tryptophan Metabolite against Cancer Growth and Metastasis.
Carcinogenesis
Induction and growth of mammary tumors after superior cervical ganglionectomy in sighted and blinded-anosmic rats.
Choriocarcinoma
Human placental trophoblasts synthesize melatonin and express its receptors.
Colitis, Ulcerative
Evaluation of enterochromaffin cells and melatonin secretion exponents in ulcerative colitis.
Ganglion Cysts
Melatonin and 5-methoxytryptophol (5-ML) in nervous and/or neurosensory structures of a gastropod mollusc (Helix aspersa maxima): synthesis and diurnal rhythms.
Medulloblastoma
Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors.
Neoplasms
ASMT Regulates Tumor Metastasis Through the Circadian Clock System in Triple-Negative Breast Cancer.
Neoplasms
Demonstration of hydroxyindole-O-methyltransferase (HIOMT) mRNA expression in pineal parenchymal tumors: histochemical in situ hybridization.
Neoplasms
Effect of TNF-alpha on the melatonin synthetic pathway in the rat pineal gland: basis for a 'feedback' of the immune response on circadian timing.
Neoplasms
Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors.
Neoplasms
Histological features and expression of enzymes implicated in melatonin synthesis in pineal parenchymal tumours and in cultured tumoural pineal cells.
Neoplasms
Inhibitory effects of superior cervical ganglionectomy on dimethylbenz(a)anthracene-induced mammary tumors in the rat.
Neoplasms
Modification of hydroxyindole-O-methyltransferase activity in experimental pineocytomas induced in hamsters by a human papovavirus (JC).
Neoplasms
Restoration of hydroxyindole O-methyltransferase levels in human cancer cells induces a tryptophan-metabolic switch and attenuates cancer progression.
Neuroectodermal Tumors, Primitive
Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors.
Pinealoma
DEMONSTRATION OF HYDROXYINDOLE-O-METHYL TRANSFERASE, MELATONIN, AND SEROTONIN IN A METASTATIC PARENCHYMATOUS PINEALOMA.
Pinealoma
Demonstration of hydroxyindole-O-methyltransferase (HIOMT) mRNA expression in pineal parenchymal tumors: histochemical in situ hybridization.
Pinealoma
Experimental and spontaneous pineal tumors: findings relating to endocrine and oncogenic factors and mechanisms.
Pinealoma
Immunoreactive S-antigen in cerebrospinal fluid: a marker of pineal parenchymal tumors?
Pinealoma
Microarray analysis reveals differential gene expression patterns in tumors of the pineal region.
Pinealoma
Modification of hydroxyindole-O-methyltransferase activity in experimental pineocytomas induced in hamsters by a human papovavirus (JC).
Retinitis Pigmentosa
Immunocytochemistry of retinitis pigmentosa retinas: localization of HIOMT immunoreactivity in surviving photoreceptor cells.
Retinoblastoma
Cyclic AMP and butyrate modulate melatonin synthesis in Y79 human retinoblastoma cells.
Retinoblastoma
Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells.
Retinoblastoma
Hydroxyindole-O-methyltransferase in Y-79 human retinoblastoma cells: effect of cell attachment.
Retinoblastoma
Regulation of AA-NAT and HIOMT gene expression by butyrate and cyclic AMP in Y79 human retinoblastoma cells.
Retinoblastoma
Retinoic acid increases hydroxyindole-O-methyltransferase activity and mRNA in human Y-79 retinoblastoma cells.
Vitamin A Deficiency
Regulation of hydroxyindole-O-methyltransferase gene expression in Japanese quail (Coturnix coturnix japonica).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.371
N-acetylserotonin
-
isoform ASMT3, pH and temperature not specified in the publication
0.864
N-acetylserotonin
-
recombinant enzyme, pH not specified in the publication, 30°C
additional information
additional information
Michaelis-Menten kinetics
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000007
-
purified GST-tagged recombinant enzyme, pH not specified in the publication, 30°C
0.000013
-
purified nontagged recombinant enzyme, pH not specified in the publication, 30°C
0.00003
-
purified nontagged recombinant enzyme, pH not specified in the publication, 30°C, at 10 mM substrate N-acetylserotonin concentration
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
8.2
7.8
both recombinant N- and C-terminal fusions of enzyme AtCOMT exhibit the highest enzyme activities at pH 7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.8
both recombinant N- and C-terminal fusions of the enzyme, no activity at pH 5.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
both recombinant N- and C-terminal fusions of enzyme AtCOMT exhibit the highest enzyme activities at pH 37°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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enzyme-associated melatonin levels increase as temperature increases, without effect on enzyme-encoding gene transcript levels. The melatonin levels in rice plants a 45°C and 55°C are 26% and 54% higher than that at 25°C, showing a peak level at 55°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
5.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene At4g35160 or AtASMT; gene AtASMT
UniProt
brenda
the ASMT gene is spliced in an alternative way to form at least three possible isoforms
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is predominantly localized in the large luteal cells of porcine corpus lutem during pregnancy
brenda
-
postovulatory, no activity in preovulatory ovarian follicle
brenda
-
CD19+ cell, CD14-CD4+ cell, CD56-CD8+ cell, CD56+ cell
brenda
the testes of control animals express the Tph1, Aanat, and Asmt and Per2 genes with 24-h rhythms in mRNA, reaching the maximal values during the dark phase. Pinealectomy abolishes and melatonin treatment restores the 24-h rhythmicity
brenda
additional information
additional information
Frog
-
not: liver, kidney, heart, lung, adrenal gland, pancreas, salivary gland, skin
brenda
additional information
-
not: liver, kidney, heart, lung, adrenal gland, pancreas, salivary gland, skin
brenda
additional information
-
temperature- and light-dependent enzyme activity and melatonin biosynthesis in rice plants, overview. The enzyme activity is increased at higher Temperature of 55°C and at darkness
brenda
additional information
-
not: liver, kidney, heart, lung, adrenal gland, pancreas, salivary gland, skin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to S-adenosyl-L-methionine dependent animal natural product O-methyltransferase
evolution
caffeic acid O-methyltransferase likely evolved from N-acetylserotonin methyltransferase by gene duplication and subsequent divergence. Caffeic acid O-methyltransferase gained a significantly higher N-acetylserotonin methyltransferase activity to produce greater amounts of melatonin for immobile plants to acclimate to the land environments. The caffeic acid O-methyltransferase genes possess more conserved substrate-binding sites at the amino acid level and more open protein conformation compared to N-acetylserotonin methyltransferase genes
malfunction
transgenic rice plants overexpressing rice caffeic acid O-methyltransferase/N-acetylserotonin O-methyltransferase show an increase in melatonin levels whereas transgenic rice plants suppressing the rice caffeic acid O-methyltransferase/N-acetylserotonin O-methyltransferase have a significant decrease on melatonin levels
malfunction
melatonin production is significantly reduced or increased when the rice plants overexpressed or suppressed the endogenous rice caffeic acid O-methyltransferase
malfunction
lack of melatonin is a risk signal and will result in diabetes, psychiatric disorders, and other diverse medical conditions
malfunction
alpha-synuclein increases the binding between microtubule-associated protein 1 light chain 3 beta and the enzyme, leading to enzyme degradation and a consequent reduction in melatonin biosynthesis
metabolism
the enzyme catalyzes the conversion of N-acetylserotonin to melatonin as the last step in melatonin biosynthesis. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
metabolism
-
the final two enzymes in the melatonin synthesis pathway in plants are serotonin N-acetyltransferase (SNAT) and N-acetylserotonin methyltransferase (ASMT), which have thermophilic characteristics
metabolism
in vivo role played by the COMT for biosynthesizing melatonin
metabolism
-
all three isozymes are involved in the biosynthesis of melatonin. the enzyme is involved in a general tryptophan metabolism pathway where it catalyzes the final reaction in the production of melatonin, converting normelatonin to melatonin (a neurohormone). The conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate in the same pathway is also catalyzed by this enzyme. In general tryptophan metabolism pathway, tryptophan functions as a biochemical precursor for serotonin
metabolism
ASMT is a key enzyme to catalyse the terminal step of melatonin (N-acetyl-5-methoxytryptamine)
metabolism
-
isoform COMT1 is involved in melatonin biosynthesis in the cytoplasm and nucleus
metabolism
-
the enzyme catalyzes the conversion of N-acetylserotonin to melatonin as the last step in melatonin biosynthesis. The enzyme exhibits no caffeic acid O-methyltransferase activity, suggesting that its function is highly specific to melatonin synthesis
-
metabolism
-
in vivo role played by the COMT for biosynthesizing melatonin
-
physiological function
-
HIOMT is required for full transcriptional activation in chicken embryonic retinal cells
physiological function
direct role of caffeic acid O-methyltransferase/N-acetylserotonin O-methyltransferase in melatonin biosynthesis in plants
physiological function
ASMT is a key enzyme to catalyse the terminal step of melatonin (N-acetyl-5-methoxytryptamine). Melatonin is related with various physiological functions, such as sleep induction, circadian rhythm regulation together with oxidative stress and immune response
physiological function
cassava bacterial blight induces the expression of transcription factor WRKY79 and heat-shock transcription factor Hsf20, and the induced WRKY79 and Hsf20 activate the expression of ASMT2 via binding to W-box and HSEs in the ASMT2 promotor, which in turn increases melatonin accumulation and confers improved disease resistance
physiological function
rice leaves treated with flavonoids and then cadmium display lower melatonin levels than the flavonoid-untreated control
physiological function
the absence of pineal melatonin in pinealectomized animals phase shifts the daily peak of Asmt mRNA expression to daytime
physiological function
-
melatonin-deficient rice, in which expression of endogenous ASMT is suppressed, exhibits accelerated senescence in detached flag leaves, as well as significantly reduced yield
physiological function
-
increased melatonin production due to enzyme overexpression in transgenic goats contributes to improved milk quality and enhanced anti-inflammatory ability compared to wild type goats
physiological function
-
enzyme isoform COMT1 overexpression results in decreased wilting in transgenic tobacco plants subjected to dehydration treatment. The combinatorial effects of the enzyme in increasing melatonin content, inducing antioxidant system, and elevating the expression of drought-related genes candeliver the drought tolerance in tobacco
physiological function
isoform ASMT9 overexpression positively impacts the apple plant's response to heat stress by improving basal thermotolerance through scavenging harmful reactive oxygen species and maintaining higher photosynthetic capacity. Isoform ASMT9 overexpression increases stomatal aperture through promoting MdWRKY33-mediated transcriptional inhibition of NCED1 and NCED3. Moreover, exogenous melatonin and overexpression of isoform ASMT9 enhances autophagic activity through promoting WRKY33-mediated transcriptional enhancement of ATG18a under heat stress
physiological function
-
ectopic expression of isoform ASMT1 in Nicotiana benthamiana significantly enhances melatonin production in transgenic plants. Compared with wild type plants, the transgenic lines exhibit a higher germination ratio, longer root length, lower degree of leaf wilting and relative water content under salt and osmotic stresses. In addition, under salt and osmotic stresses, overexpression of ASMT1 improves proline and malondialdehyde contents, increases the activity of antioxidant enzymes and decreases the accumulation of reactive oxygen species
physiological function
overexpression of isoform ASMT9 increases melatonin biosynthesis and improves water-use efficiency in transgenic apple
physiological function
-
overexpression of COMT1 significantly increases melatonin contents, COMT1 knockout decreases melatonin contents in watermelon calli. In Arabidopsis thaliana,overexpression of COMT1 enhances transgenic Arabidopsis tolerance against abiotic stress
physiological function
COMT is involved in melatonin biosynthesis and significantly delays leaf senescence at the grain filling stage by inhibiting degradation of chlorophyll and chloroplast. Number and size of vascular bundles in the culms and leaves are significantly increased in COMT-overexpressing plants. COMT is a positive regulator of grain yield, and overexpression of COMT increases grain yield per plant even in a high-yield variety background
physiological function
-
enzyme overexpression likely enhances the resistance of transgenic sheep to brucellosis
physiological function
overexpression of LCOMT gene in Arabidopsis thaliana confers enhanced drought tolerance, i.e. elevated lignin and melatonin levels, increased chlorophyll and carotenoid content, heightened activities of antioxidant enzymes peroxidase, catalase, and superoxide dismutase, and reduced malondialdehyde and hydrogen peroxide accumulation
physiological function
-
isoforms ASMT3, ASMT44, ASMT17, and ASMT7 are involved in embryo development, heat, drought, aphid, and soybean cyst nematode infections, respectively. The enzyme demonstrates auxin-like activities by regulating the genes involved in auxin transporter (WAT1 and NRT1/PTR) and auxin-responsive protein during developmental and biotic stress. Isoform ASMT44 is associated with stress response, transcription regulation, hormone signalling, calcium ion binding, protein kinase activity, and carbon metabolism
physiological function
enzyme overexpression leads to a series of phenotypic changes, including vigorous growth, increased plant height, enlarged leaves and robust stems with increased cell sizes, cell numbers and vascular bundles, as well as more branches. Also the flavonoid content and lignin composition of syringyl to guaiacyl ratio are decreased and the cellulose content is increased in transgenic alfalfa overexpressing isoform ASMT1
physiological function
enzyme overexpression improves the adaptation of apple leaves to salt stress, primarily by increasing melatonin concentration, maintaining a high photosynthetic capacity, reducing reactive oxygen species accumulation, and maintaining normal ion homeostasis. The transgenic apple lines show reduced salt damage symptoms, lower relative electrolyte leakage, and less total chlorophyll loss from leaves under salt stress
physiological function
-
isoforms ASMT1 and ASMT3 overexpression in Arabidopsis mutants causes 1.5-2fold higher melatonin content than in mutant and wild type plants. The endogenous reactive oxygen species in transgenic plants is significantly lower than ROS in mutant and wild type plants, suggesting higher drought tolerance
physiological function
-
isoforms ASMT2 and ASMT3 positively regulate endogenous melatonin level and autophagic activity by interacting with theautophagy-associated genes ATG8b, 8c, and 8e
additional information
-
the daily melatonin levels in field-grown rice plants are unaffected as the positive effect of the relatively high temperature during the day is counteracted by the negative effect of the high light. The opposite effect occurs during the night, in which the positive effect of darkness on melatonin synthesis is counteracted by the negative effect of a low temperature
additional information
-
structural homology molecular modeling and model evaluation, molecular dynamics simulation, overview. Active site determination and modeling of ligand binding by the enzyme
additional information
roles of several residues around the active sites and methyl-transfer mechanism of human N-acetylserotonin methyltransferase, density function theory method, overview. residues H255, D256, E311, and R252 play an important role in reducing the barrier height and inducing methyl transfer. Some residues around the SAM in the centre of active site are essential factors to influence the mechanism and barrier height
Show AA Sequence and Transmembrane Helices (1713 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38000
39000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D269A
mutation leads to a 94.29% decrease in activity towards caffeic acid and a 16.56% decrease for N-acetylserotonin
F171A
mutation decrease activity of towards caffeic acid by 81.90%, and affinity towards N-acetylserotonin by 10.86%
additional information
additional information
ectopic overexpression of the enzyme in rice results in increased ASMT enzyme activity and melatonin production
additional information
-
ectopic overexpression of the enzyme in rice results in increased ASMT enzyme activity and melatonin production
additional information
construction of an Arabidopsis thaliana comt knockout mutant (SALK_002373) with T-DNA inserted at the third exon. The comt mutant shows no detectable COMT transcript and exhibits a 20fold less COMT activity relative over the wild type, the phenotypes such as growth and fertility are indistinguishable from the wild-type plants
additional information
-
construction of an Arabidopsis thaliana comt knockout mutant (SALK_002373) with T-DNA inserted at the third exon. The comt mutant shows no detectable COMT transcript and exhibits a 20fold less COMT activity relative over the wild type, the phenotypes such as growth and fertility are indistinguishable from the wild-type plants
additional information
-
ectopic overexpression of the enzyme in rice results in increased ASMT enzyme activity and melatonin production
-
additional information
-
construction of an Arabidopsis thaliana comt knockout mutant (SALK_002373) with T-DNA inserted at the third exon. The comt mutant shows no detectable COMT transcript and exhibits a 20fold less COMT activity relative over the wild type, the phenotypes such as growth and fertility are indistinguishable from the wild-type plants
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 96 h, pineal enzyme stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
reombinant N-and C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatograpy
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
FreeStyle 293 expression system used for cellular expression, His-tagged protein synthesized in the Rapid translation system RTS500
gene cloning, DNA and amino acid sequence determination and analysis, the At4g35160 gene exhibits the highest sequence identity (31%) to the rice ASMT gene, followed by the At1g76790 gene with 29% sequence identity, phylogenetic analysis. The recombinant proteins are recombinantly expressed from the two Arabidopsis genes. The At4g35160 recombinant protein exhibits ASMT enzyme activity, but the At1g76790 recombinant protein does not. Recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene comt, recombinant expression in Escherichia coli strain BL21(DE3), the N-terminal His-tagged AtCOMT is more highly expressed in soluble form than the C-terminal His-tagged AtCOMT
gene OsASMT, DNA and amino acid sequence determination and analysis, recombinant expression of GST-tagged and of nontagged enzyme in Escherichia coli strain BL21(DE3), expression of N- or C-terminally His-tagged enzyme is not successful
-
gene OsCOMT, recombinant His6-tagged enzyme expression in Escherichia coli strain BL21(DE3), generation of transgenic Nicotiana benthamiana plants and Oryza sativa plants expressing the enzyme using the Agrobacterium tumefaciens strains GV2260 and LBA4404 transfection method
isoforms ASMT1 and ASMT3 are expressed in Escherichia coli strain BL21 (DE3) and in Arabidopsis thaliana
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-synuclein reduces the level and activity of the enzyme in the pineal gland and in the cell cultures. Microtubule-associated protein 1 light chain 3 beta is involved in the degradation of the enzyme
AtASMT transcripts are induced by cadmium treatment in Arabidopsis thaliana followed by increased melatonin synthesis
COMT1 expression is upregulated by cold, drought, and salt stress, accompanied by increases in melatonin contents
-
enzyme-associated melatonin levels increase as temperature increases when rice seedlings are exposed to various temperatures for 1 hr, but temperature-dependent increase in melatonin synthesis is only closely associated with an increase in both SNAT and ASMT activities, but not with transcript levels of melatonin biosynthetic genes. The relative melatonin levels are higher in the dark, exposure of rice seedlings to 1 hr darkness at 55°C results in a melatonin yield of 4.9 ng/g fresh weight, compared with 2.95 ng/g fresh weight under light conditions
-
In retinal cells the mutation of the YY1-binding site decreases the HIOMT promoter activity by 70%
-
the enzyme is significantly induced by salt (highest peak after 6 h at 200 mM NaCl) and osmotic stresses (highest peak after 4 h at 200 mM mannitol)
-
the expression level in submandibular gland is higher in the dark period compared with the light period
-
the mRNA expression for HIOMT is only slightly increased at day 0 upon ulcer induction when compared with that in the intact mucosa, but at day 8 after ulcer formation, this expression of HIOMT is significantly enhanced, particularly at the ulcer areas in rats treated with melatonin or L-tryptophan
-
the rat Crx transcription factor is able to activate the HIOMT promoter in transfected HEK-293 cells
-
the transcripts of transcriptional activator WRKY79, heat-shock transcription factor Hsf20, and ASMT2 are all regulated by a 22-amino acid flagellin peptide (flg22) and by Xanthomonas axonopodis pv manihotis
there is an age-related decline in rat extrapineal melatonin synthesis with a consequent HIOMT functionality decrease in spleen, liver and heart during physiological aging, in the thymus HIOMT expression reveals no significant alterations with age
-
AtASMT transcripts are induced by cadmium treatment in Arabidopsis thaliana followed by increased melatonin synthesis
AtASMT transcripts are induced by cadmium treatment in Arabidopsis thaliana followed by increased melatonin synthesis
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
target in genetic engineering to achieve crop improvement under changing environmental conditions
analysis
the standard radio-chemical assay is successful for pineal HIOMT only, whereas specific homogenization buffers and HPLC are required to detect retinal activity
synthesis
recombinant Escherichia coli expressing sheep serotonin N-acetyltransferase with rice caffeic acid O-methyltransferase produces 1.46 mg/L of melatonin in a culture medium, in response to 1 mM serotonin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Rattus norvegicus, Gallus gallus, Frog
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Kuwano, R.; Takahashi, Y.
Binding of S-adenosylhomocysteine to hydroxyindole O-methyltransferase
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Bos taurus
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Inactivation of rat pineal hydroxyindole-O-methyltransferase by disulfide-containing compounds
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Rattus norvegicus
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Bos taurus, Rattus norvegicus, Gallus gallus, Ovis aries
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Some properties of pineal gland hydroxyindole-O-methyltransferase from black rhinoceros (Diceros bicornis)
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Diceros bicornis
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Bos taurus
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1983
Bos taurus, Gallus gallus
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Oncorhynchus tshawytscha
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Purification of bovine pineal hydroxyindole O-methyltransferase by immunoadsorption chromatography
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Bos taurus
brenda
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Biochem. Pharmacol.
25
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1976
Rattus norvegicus
brenda
Karahasanoglu, A.M.; Ozand, P.T.
The purification and properties of bovine pineal S-adenosylmethionine: N-acetylserotonin O-methyl transferase
J. Neurochem.
19
411-430
1972
Bos taurus
brenda
Tedesco, S.C.; Moron, D.J.; Reiter, R.J.
Hydroxyindole-O-methyltransferase activity in the pineal gland of the muskox (Ovibos moschatus)
J. Pineal Res.
16
121-126
1994
Ovibos moschatus
brenda
Benyassi, A.; Schwartz, C.; Ducouret, B.; Falcon, J.
Glucocorticoid receptors and serotonin N-acetyltransferase activity in the fish pineal organ
NeuroReport
12
889-892
2001
Oncorhynchus mykiss
brenda
Ribelayga, C.; Gauer, F.; Calgari, C.; Pevet, P.; Simonneaux, V.
Photoneural regulation of rat pineal hydroxyindole-O-methyltransferase (HIOMT) messenger ribonucleic acid expression: an analysis of its complex relationship with HIOMT activity
Endocrinology
140
1375-1384
1999
Rattus norvegicus
brenda
Bernard, M.; Donohue, S.J.; Klein, D.C.
Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells
Brain Res.
696
37-48
1995
Homo sapiens
brenda
Itoh, M.T.; Ishizuka, B.; Kudo, Y.; Fusama, S.; Amemiya, A.; Sumi, Y.
Detection of melatonin and serotonin N-acetyltransferase and hydroxyindole-O-methyltransferase activities in rat ovary
Mol. Cell. Endocrinol.
136
7-13
1997
Rattus norvegicus
brenda
Bernard, M.; Klein, D.C.
Retinoic acid increases hydroxyindole-O-methyltransferase activity and mRNA in human Y-79 retinoblastoma cells
J. Neurochem.
67
1032-1038
1996
Homo sapiens
brenda
Ishio, S.; Yamada, H.; Craft, C.M.; Moriyama, Y.
Hydroxyindole-O-methyltransferase is another target for L-glutamate-evoked inhibition of melatonin synthesis in rat pinealocytes
Brain Res.
850
73-78
1999
Rattus norvegicus
brenda
Lewy, H.; Massot, O.; Touitou, Y.
Magnetic field (50 Hz) increases N-acetyltransferase, hydroxy-indole-O-methyltransferase activity and melatonin release through an indirect pathway
Int. J. Radiat. Biol.
79
431-435
2003
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Pozo, D.; Garcia-Maurino, S.; Guerrero, J.M.; Calvo, J.R.
mRNA expression of nuclear receptor RZR/RORalpha, melatonin membrane receptor MT, and hydroxindole-O-methyltransferase in different populations of human immune cells
J. Pineal Res.
37
48-54
2004
Homo sapiens
brenda
Olszanska, B.; Majewski, P.; Lewczuk, B.; Stepinska, U.
Melatonin and its synthesizing enzymes (arylalkylamine N-acetyltransferase-like and hydroxyindole-O-methyltransferase) in avian eggs and early embryos
J. Pineal Res.
43
310-318
2007
Coturnix japonica
brenda
Sanchez-Hidalgo, M.; de la Lastra, C.A.; Carrascosa-Salmoral, M.P.; Naranjo, M.C.; Gomez-Corvera, A.; Caballero, B.; Guerrero, J.M.
Age-related changes in melatonin synthesis in rat extrapineal tissues
Exp. Gerontol.
44
328-334
2009
Rattus norvegicus
brenda
Bernard, M.; Voisin, P.
Photoreceptor-specific expression, light-dependent localization, and transcriptional targets of the zinc-finger protein Yin Yang 1 in the chicken retina
J. Neurochem.
105
595-604
2008
Gallus gallus
brenda
Konturek, P.C.; Konturek, S.J.; Burnat, G.; Brzozowski, T.; Brzozowska, I.; Reiter, R.J.
Dynamic physiological and molecular changes in gastric ulcer healing achieved by melatonin and its precursor L-tryptophan in rats
J. Pineal Res.
45
180-190
2008
Rattus norvegicus
brenda
Zmijewski, M.A.; Sweatman, T.W.; Slominski, A.T.
The melatonin-producing system is fully functional in retinal pigment epithelium (ARPE-19)
Mol. Cell. Endocrinol.
307
211-216
2009
Homo sapiens
brenda
Velarde, E.; Cerda-Reverter, J.M.; Alonso-Gomez, A.L.; Sanchez, E.; Isorna, E.; Delgado, M.J.
Melatonin-synthesizing enzymes in pineal, retina, liver, and gut of the goldfish (Carassius): mRNA expression pattern and regulation of daily rhythms by lighting conditions
Chronobiol. Int.
27
1178-1201
2010
Carassius auratus
brenda
Shimozuma, M.; Tokuyama, R.; Tatehara, S.; Umeki, H.; Ide, S.; Mishima, K.; Saito, I.; Satomura, K.
Expression and cellular localizaion of melatonin-synthesizing enzymes in rat and human salivary glands
Histochem. Cell Biol.
135
389-396
2011
Homo sapiens, Rattus norvegicus
brenda
Fukuda, T.; Akiyama, N.; Ikegami, M.; Takahashi, H.; Sasaki, A.; Oka, H.; Komori, T.; Tanaka, Y.; Nakazato, Y.; Akimoto, J.; Tanaka, M.; Okada, Y.; Saito, S.
Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors
J. Neuropathol. Exp. Neurol.
69
498-510
2010
Homo sapiens (P46597), Homo sapiens
brenda
Byeon, Y.; Choi, G.H.; Lee, H.Y.; Back, K.
Melatonin biosynthesis requires N-acetylserotonin methyltransferase activity of caffeic acid O-methyltransferase in rice
J. Exp. Bot.
66
6917-6925
2015
Oryza sativa (Q6ZD89), Oryza sativa
brenda
Azam, S.; Saroosh, A.; Zaman, N.; Raza, S.
Role of N-acetylserotonin O-methyltransferase in bipolar disorders and its dynamics
J. Mol. Liq.
182
25-31
2013
Homo sapiens
-
brenda
Park, S.; Byeon, Y.; Kim, Y.S.; Back, K.
Kinetic analysis of purified recombinant rice N-acetylserotonin methyltransferase and peak melatonin production in etiolated rice shoots
J. Pineal Res.
54
139-144
2013
Oryza sativa
brenda
Byeon, Y.; Back, K.
Melatonin synthesis in rice seedlings in vivo is enhanced at high temperatures and under dark conditions due to increased serotonin N-acetyltransferase and N-acetylserotonin methyltransferase activities
J. Pineal Res.
56
189-195
2014
Oryza sativa
brenda
Byeon, Y.; Lee, H.Y.; Lee, K.; Back, K.
Caffeic acid O-methyltransferase is involved in the synthesis of melatonin by methylating N-acetylserotonin in Arabidopsis
J. Pineal Res.
57
219-227
2014
Arabidopsis thaliana (Q9T003), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9T003)
brenda
Byeon, Y.; Lee, H.J.; Lee, H.Y.; Back, K.
Cloning and functional characterization of the Arabidopsis N-acetylserotonin O-methyltransferase responsible for melatonin synthesis
J. Pineal Res.
60
65-73
2015
Arabidopsis thaliana (Q9T003), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9T003)
brenda
Wang, L.; Zhang, T.; Li, J.; He, C.; He, H.; Zhang, J.
Catalytic mechanism of human N-acetylserotonin methyltransferase: a theoretical investigation
Mol. Phys.
113
3438-3449
2015
Homo sapiens (P46597)
-
brenda
Byeon, Y.; Back, K.
Melatonin production in Escherichia coli by dual expression of serotonin N-acetyltransferase and caffeic acid O-methyltransferase
Appl. Microbiol. Biotechnol.
100
6683-6691
2016
Oryza sativa Japonica Group (Q6ZD89)
brenda
Betti, L.; Palego, L.; Demontis, G.C.; Miraglia, F.; Giannaccini, G.
Hydroxyindole-O-methyltransferase (HIOMT) activity in the retina of melatonin-proficient mice
Heliyon
5
e02417
2019
Mus musculus (D3KU66), Mus musculus
brenda
Byeon, Y.; Back, K.
Low melatonin production by suppression of either serotonin N-acetyltransferase or N-acetylserotonin methyltransferase in rice causes seedling growth retardation with yield penalty, abiotic stress susceptibility, and enhanced coleoptile growth under anoxi
J. Pineal Res.
60
348-359
2016
Oryza sativa
brenda
Wei, Y.; Liu, G.; Chang, Y.; Lin, D.; Reiter, R.J.; He, C.; Shi, H.
Melatonin biosynthesis enzymes recruit WRKY transcription factors to regulate melatonin accumulation and transcriptional activity on W-box in cassava
J. Pineal Res.
65
e12487
2018
Manihot esculenta (A0A193DSQ2), Manihot esculenta
brenda
Lee, K.; Hwang, O.J.; Reiter, R.J.; Back, K.
Flavonoids inhibit both rice and sheep serotonin N-acetyltransferases and reduce melatonin levels in plants
J. Pineal Res.
65
e12512
2018
Oryza sativa Japonica Group (Q6ZD89)
brenda
Coelho, L.A.; Andrade-Silva, J.; Motta-Teixeira, L.C.; Amaral, F.G.; Reiter, R.J.; Cipolla-Neto, J.
The absence of pineal melatonin abolishes the daily rhythm of Tph1 (tryptophan hydroxylase 1), Asmt (acetylserotonin O-methyltransferase), and Aanat (aralkylamine N-acetyltransferase) mRNA expressions in rat testes
Mol. Neurobiol.
56
7800-7809
2019
Rattus norvegicus (B3GSH5)
brenda
Zhang, W.L.; Zhang, Z.L.; Peng, J.; Yang, S.T.; Chen, J.X.; Wang, C.X.; Tong, D.W.
Expression of arylalkylamine N-acetyltransferase (AANAT) and acetylserotonin O-methyltransferase (ASMT) in the corpus luteum of pregnant sows and synthesis of melatonin in luteal cells
Cell Tissue Res.
388
167-179
2022
Sus scrofa
brenda
Jia, C.; Tian, L.; Cheng, C.; Zhang, J.; Al-Nusaif, M.; Li, T.; Yang, H.; Lin, Y.; Li, S.; Le, W.
alpha-Synuclein reduces acetylserotonin O-methyltransferase mediated melatonin biosynthesis by microtubule-associated protein 1 light chain 3 beta-related degradation pathway
Cell. Mol. Life Sci.
81
61
2024
Mus musculus (D3KU66)
brenda
Li, G.; Lv, D.; Yao, Y.; Wu, H.; Wang, J.; Deng, S.; Song, Y.; Guan, S.; Wang, L.; Ma, W.; Yang, H.; Yan, L.; Zhang, J.; Ji, P.; Zhang, L.; Lian, Z.; Liu, G.
Overexpression of ASMT likely enhances the resistance of transgenic sheep to brucellosis by influencing immune-related signaling pathways and gut microbiota
FASEB J.
35
e21783
2021
Ovis aries
brenda
Cen, H.; Wang, T.; Liu, H.; Wang, H.; Tian, D.; Li, X.; Cui, X.; Guan, C.; Zang, H.; Li, M.; Zhang, Y.
Overexpression of MsASMT1 promotes plant growth and decreases flavonoids biosynthesis in transgenic alfalfa (Medicago sativa L.)
Front. Plant Sci.
11
489
2020
Medicago sativa (A0A649WZ66)
brenda
Kumar, G.; Arya, M.; Padma, R.; Puthusseri, B.; Giridhar, P.
Distinct GmASMTs are involved in regulating transcription factors and signalling cross-talk across embryo development, biotic, and abiotic stress in soybean
Front. Plant Sci.
13
948901
2022
Glycine max
brenda
Huang, E.; Tang, J.; Song, S.; Yan, H.; Yu, X.; Luo, C.; Chen, Y.; Ji, H.; Chen, A.; Zhou, J.; Liao, H.
Caffeic acid O-methyltransferase from Ligusticum chuanxiong alleviates drought stress, and improves lignin and melatonin biosynthesis
Front. Plant Sci.
15
1458296
2024
Conioselinum anthriscoides (A0A0K1YW34)
brenda
Chang, J.; Guo, Y.; Yan, J.; Zhang, Z.; Yuan, L.; Wei, C.; Zhang, Y.; Ma, J.; Yang, J.; Zhang, X.; Li, H.
The role of watermelon caffeic acid O-methyltransferase (ClCOMT1) in melatonin biosynthesis and abiotic stress tolerance
Hortic. Res.
8
210
2021
Citrullus lanatus
brenda
Tan, K.; Zheng, J.; Liu, C.; Liu, X.; Liu, X.; Gao, T.; Song, X.; Wei, Z.; Ma, F.; Li, C.
Heterologous expression of the melatonin-related gene HIOMT improves salt tolerance in Malus domestica
Int. J. Mol. Sci.
22
12425
2021
Homo sapiens (P46597)
brenda
Wei, Y.; Bai, Y.; Cheng, X.; Zhu, B.; Reiter, R.J.; Shi, H.
The dual roles of melatonin biosynthesis enzymes in the coordination of melatonin biosynthesis and autophagy in cassava
J. Pineal Res.
69
e12652
2020
Manihot esculenta
brenda
Zhou, W.; Wang, Y.; Li, B.; Petijova, L.; Hu, S.; Zhang, Q.; Niu, J.; Wang, D.; Wang, S.; Dong, Y.; Cellarova, E.; Wang, Z.
Whole-genome sequence data of Hypericum perforatum and functional characterization of melatonin biosynthesis by N-acetylserotonin O-methyltransferase
J. Pineal Res.
70
e12709
2021
Hypericum perforatum
brenda
Zhao, D.; Yao, Z.; Zhang, J.; Zhang, R.; Mou, Z.; Zhang, X.; Li, Z.; Feng, X.; Chen, S.; Reiter, R.J.
Melatonin synthesis genes N-acetylserotonin methyltransferases evolved into caffeic acid O-methyltransferases and both assisted in plant terrestrialization
J. Pineal Res.
71
e12737
2021
Arabidopsis thaliana (Q9FK25), Oryza sativa Japonica Group (Q6EPG8)
brenda
Wu, H.; Cui, X.; Guan, S.; Li, G.; Yao, Y.; Wu, H.; Zhang, J.; Zhang, X.; Yu, T.; Li, Y.; Lian, Z.; Zhang, L.; Liu, G.
The improved milk quality and enhanced anti-inflammatory effect in acetylserotonin-O-methyltransferase (ASMT) overexpressed goats An association with the elevated endogenous melatonin production
Molecules
27
572
2022
Capra hircus
brenda
Yao, Z.; Zhang, X.; Liang, Y.; Zhang, J.; Xu, Y.; Chen, S.; Zhao, D.
NtCOMT1 responsible for phytomelatonin biosynthesis confers drought tolerance in Nicotiana tabacum
Phytochemistry
202
113306
2022
Nicotiana tabacum
brenda
Huangfu, L.; Chen, R.; Lu, Y.; Zhang, E.; Miao, J.; Zuo, Z.; Zhao, Y.; Zhu, M.; Zhang, Z.; Li, P.; Xu, Y.; Yao, Y.; Liang, G.; Xu, C.; Zhou, Y.; Yang, Z.
OsCOMT, encoding a caffeic acid O-methyltransferase in melatonin biosynthesis, increases rice grain yield through dual regulation of leaf senescence and vascular development
Plant Biotechnol. J.
20
1122-1139
2022
Oryza sativa Japonica Group (Q6ZD89)
brenda
Gao, T.; Zhang, D.; Shen, W.; Xu, S.; Jia, X.; Liu, X.; Tan, K.; Zhou, Y.; Zhang, Z.; Ma, F.; Li, C.
MdASMT9-mediated melatonin biosynthesis enhances basal thermotolerance in apple plants
Plant Cell Environ.
47
751-764
2024
Malus domestica (A0A344X471)
brenda
Yu, Y.; Ni, Y.; Qiao, T.; Ji, X.; Xu, J.; Li, B.; Sun, Q.
Overexpression of VvASMT1 from grapevine enhanced salt and osmotic stress tolerance in Nicotiana benthamiana
PLoS ONE
17
e0269028
2022
Vitis vinifera
brenda
Zhou, K.; Li, Y.; Hu, L.; Zhang, J.; Yue, H.; Yang, S.; Liu, Y.; Gong, X.; Ma, F.
Overexpression of MdASMT9, an N-acetylserotonin methyltransferase gene, increases melatonin biosynthesis and improves water-use efficiency in transgenic apple
Tree Physiol.
42
1114-1126
2022
Malus domestica (A0A344X471)
brenda
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