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Information on EC 2.1.1.4 - acetylserotonin O-methyltransferase and Organism(s) Homo sapiens
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2.1.1.4 acetylserotonin O-methyltransferaseIUBMB Comments
Some other hydroxyindoles also act as acceptor, but more slowly.
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Word Map
- 2.1.1.4
- melatonin
-
pineal
- n-acetyltransferase
-
rhythm
- retina
-
circadian
-
nocturnal
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night
- arylalkylamine
- pinealocytes
-
diurnal
- photoreceptors
-
photoperiodic
-
melatoninergic
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harderian
-
melatonin-synthesizing
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daytime
-
nighttime
- 5-hydroxytryptophan
- aa-nat
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arylalkylamine-n-acetyltransferase
- 5-methoxytryptophan
- 5-methoxytryptamine
- 5-hydroxyindole
- n-acetyl-5-methoxytryptamine
-
pinealectomized
- serotonin-n-acetyltransferase
-
5-hydroxyindoleacetic
- 5-methoxyindoles
- analysis
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light:dark
- synthesis
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ganglionectomy
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extrapineal
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
hiomt, hydroxyindole-o-methyltransferase, hydroxyindole o-methyltransferase, n-acetylserotonin methyltransferase, acetylserotonin o-methyltransferase, n-acetylserotonin o-methyltransferase, hydroxyindole-o-methyl transferase, asmt2, acetylserotonin methyltransferase, asmt1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylserotonin methyltransferase
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-
-
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ASMT
HIOMT
hydroxyindole methyltransferase
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-
-
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hydroxyindole O-methyltransferase
hydroxyindole-O-methyl transferase
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-
-
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hydroxyindole-O-methyltransferase
methyltransferase, acetylserotonin
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-
-
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N-acetylserotonin O-methyltransferase
ASMT
-
-
-
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HIOMT
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-
-
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hydroxyindole O-methyltransferase
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-
-
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N-acetylserotonin O-methyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
modeling of the catalytic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
O-methylation
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
CAS REGISTRY NUMBER
COMMENTARY
9029-77-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
-
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
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-
-
-
?
additional information
?
-
-
the enzyme also catalyzes the conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate
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-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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-
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
-
-
-
-
?
additional information
?
-
-
the enzyme also catalyzes the conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
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-
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
retinoic acid stereoisomers induce an increase in activity and mRNA level
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the ASMT gene is spliced in an alternative way to form at least three possible isoforms
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CD19+ cell, CD14-CD4+ cell, CD56-CD8+ cell, CD56+ cell
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to S-adenosyl-L-methionine dependent animal natural product O-methyltransferase
malfunction
lack of melatonin is a risk signal and will result in diabetes, psychiatric disorders, and other diverse medical conditions
metabolism
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
additional information
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)
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
additional information
-
structural homology molecular modeling and model evaluation, molecular dynamics simulation, overview. Active site determination and modeling of ligand binding by the enzyme
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ASMT_HUMAN
345
0
38453
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
FreeStyle 293 expression system used for cellular expression, His-tagged protein synthesized in the Rapid translation system RTS500
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
-
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)
-
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