Aralkylamine N-acetyltransferase
class of enzymes
Aralkylamine N-acetyltransferase (AANAT) (EC 2.3.1.87), also known as arylalkylamine N-acetyltransferase or serotonin N-acetyltransferase (SNAT), is an enzyme that is involved in the day/night rhythmic production of melatonin, by modification of serotonin. It is in humans encoded by the ~2.5 kb AANAT gene containing four exons, located on chromosome 17q25. The gene is translated into a 23 kDa large enzyme. It is well conserved through evolution and the human form of the protein is 80 percent identical to sheep and rat AANAT. It is an acetyl-CoA-dependent enzyme of the GCN5-related family of N-acetyltransferases (GNATs). It may contribute to multifactorial genetic diseases such as altered behavior in sleep/wake cycle and research is ongoing with the aim of developing drugs that regulate AANAT function.
Nomenclature
The systematic name of this enzyme class is acetyl-CoA:2-arylethylamine N-acetyltransferase. Other names in common use include:
AANAT
Arylalkylamine N-acetyltransferase
Melatonin rhythm enzyme
Serotonin acetylase
Serotonin acetyltransferase
Serotonin N-acetyltransferase
The officially accepted name is aralkylamine N-acetyltransferase.
Function and mechanism
Tissue distribution
The AANAT mRNA transcript is mainly expressed in the central nervous system (CNS). It is detectable at low levels in several brain regions including the pituitary gland as well as in the retina. It is most highly abundant in the pineal gland which is the site of melatonin synthesis.
Begin with the source’s own compact description: “Aralkylamine N-acetyltransferase” is class of enzymes. The dossier treats that line as a proposition to test through Aralkylamine, N-acetyltransferase and class, not as a finished interpretation.
Why this record matters
The phrase “class of enzymes” supplies a clear boundary for inquiry. It also exposes the unanswered questions: who defined that boundary, when it became stable and which sources sit outside it.
The citation trail is more important than the brevity of the summary: it shows where individual claims can be examined in context. The source revision retrieved here is dated Sep 8, 2026. The linked authority identifier is Q416754. None of the 0 selected statements returned an explicit reference.
Overview language is designed for orientation and should not be treated as a substitute for the evidence cited beneath it. The source lead contains qualifying language; that uncertainty should survive quotation, summary and reuse. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.
How to read it
Use the entry as an orientation point, then follow its citations and revision history. Names, dates and institutional relationships should be checked against the original record.
- Subject orientation
- Search vocabulary
- Locating named sources
The closest primary source, responsible institution and strongest cited specialist reference.
Three-step research path
- Establish the record: confirm the title “Aralkylamine N-acetyltransferase”, its source revision and the description used here.
- Expand the search: follow Aralkylamine N-acetyltransferase primary sources, Aralkylamine N-acetyltransferase archive and Aralkylamine research across catalogues and specialist indexes.
- Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.
Questions for further research
- Which source most directly establishes the central claim about “Aralkylamine N-acetyltransferase”?
- Which cited source is closest to the event, object or claim?
- What terminology or title could unlock a more precise catalogue search?
Search terms from this dossier
This entry incorporates text from “Aralkylamine N-acetyltransferase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.