Acetylserotonin-O-methyltransferase
| Acetylserotonin O-methyltransferase | ||
|---|---|---|
| other names |
Hydroxyindole O-methyltransferase, HIOMT |
|
| Properties of human protein | ||
| Mass / length primary structure | 345 amino acids , 38,453 Da | |
| Identifier | ||
| External IDs | ||
| Enzyme classification | ||
| EC, category | 2.1.1.4 | |
| Orthologue (human) | ||
| Entrez | 438 | |
| Ensemble | ENSG00000196433 | |
| UniProt | P46597 | |
| Refseq (mRNA) | NM_001171038.1 | |
| Refseq (protein) | NP_001164509.1 | |
| PubMed search |
438
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Acetylserotonin-O-methyltransferase (ASMT, EC 2.1.1.4) is the enzyme that methylates N -acetylserotonin with S- adenosylmethionine , resulting in melatonin .
properties
The isoform 1 catalyzes the reaction:
S-adenosyl-L-methionine + N-acetylserotonin → S-adenosyl-L-homocysteine + melatonin
Isoforms 2 and 3 have no enzymatic activity .
Acetylserotonin-O-methyltransferase is produced in large quantities in the pineal gland . Only ASMT mRNA is found in the retina , but not the protein .
Individual evidence
- ↑ a b BRENDA - Information on EC 2.1.1.4 - acetylserotonin O-methyltransferase. Retrieved May 18, 2018 .
- ↑ a b c ASMT - Acetylserotonin O-methyltransferase - Homo sapiens (Human) - ASMT gene & protein. In: uniprot.org. June 20, 2018, accessed May 23, 2018 .
- ↑ IR Rodriguez, K. Mazuruk, TJ Schoen, GJ Chader: Structural analysis of the human hydroxyindole-O-methyltransferase gene. Presence of two distinct promoters. In: Journal of Biological Chemistry . Volume 269, Number 50, December 1994, pp. 31969-31977, PMID 7989373 .
- ↑ M. Bernard, SJ Donohue, DC Klein: Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells. In: Brain Research . Volume 696, Number 1-2, October 1995, pp. 37-48, PMID 8574683 .