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Information on EC 2.1.1.4 - acetylserotonin O-methyltransferase and Organism(s) Homo sapiens and UniProt Accession P46597

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     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.
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This record set is specific for:
Homo sapiens
UNIPROT: P46597
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxyindole O-methyltransferase
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hydroxyindole-O-methyltransferase
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N-acetylserotonin methyltransferase
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acetylserotonin methyltransferase
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-
-
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HIOMT
hydroxindole-O-methyltransferase
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hydroxyindole methyltransferase
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-
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hydroxyindole O-methyltransferase
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hydroxyindole-O-methyl transferase
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-
-
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hydroxyindole-O-methyltransferase
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methyltransferase, acetylserotonin
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-
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N-acetylserotonin O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin
show the reaction diagram
modeling of the catalytic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
-
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O-methylation
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-
-
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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 hide
9029-77-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
show the reaction diagram
-
-
-
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme also catalyzes the conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
show the reaction diagram
-
-
-
?
N-acetylserotonin + S-adenosyl-L-methionine
S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + N-acetylserotonin
S-adenosyl-L-homocysteine + melatonin
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme also catalyzes the conversion of 5-hydroxyindoleacetate to 5-methoxyindoleacetate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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S-adenosyl-L-methionine
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetylserotonin
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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retinoic acid stereoisomers induce an increase in activity and mRNA level
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
pineal parenchymal cell tumor
Manually annotated by BRENDA team
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CD19+ cell, CD14-CD4+ cell, CD56-CD8+ cell, CD56+ cell
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
ASMT is a key enzyme to catalyse the terminal step of melatonin (N-acetyl-5-methoxytryptamine)
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
metabolism
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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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASMT_HUMAN
345
0
38453
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
x * 42000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme crystal structure, PDB ID 4A6E, analysis and structure modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team