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Aralkylamine N-acetyltransferase

serotonin N-acetyltransferase, arylalkylamine N-acetyltransferase, AANAT
regulates melatonin biosynthesis; may play a role in circadian rhythm and response to photoperiod [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Arylamine N-Acetyltransferase, CLOCK, hydroxyindole-O-methyltransferase, CAN, ACID
Papers on serotonin N-acetyltransferase
Evidence of melatonin synthesis in the ram reproductive tract.
Casao et al., Zaragoza, Spain. In Andrology, Feb 2016
To further corroborate an extrapineal secretion of melatonin, the presence of the two key enzymes involved in melatonin synthesis, arylalkylamine-N-acetyltransferase (AANAT) and N-acetylserotonin-O-methyltransferase (ASMT) was analyzed by RT-PCR, q-PCR and Western-blot in ram testes, epididymis, and accessory glands.
Molecular Evolution of Aralkylamine N-Acetyltransferase in Fish: A Genomic Survey.
Shi et al., Shenzhen, China. In Int J Mol Sci, Dec 2015
Several important sites of AANAT proteins and regulatory elements of aanat genes were analyzed for structural comparison and functional forecasting, respectively, which provides insights into the molecular evolution of the differences between AANAT1 and AANAT2.
Effects of starvation, re-feeding and timing of food supply on daily rhythm features of gut melatonin in carp (Catla catla).
Maitra et al., India. In Chronobiol Int, Nov 2015
Influences of starvation, re-feeding and time of food supply on daily rhythm features of melatonin (5-methoxy-N-acetyltryptamine) and its key regulator AANAT (arylalkylamine N-acetyltransferase) protein in the gut tissues were separately evaluated in carp Catla catla.
Heterogeneous ribonucleoprotein R regulates arylalkylamine N-acetyltransferase synthesis via internal ribosomal entry site-mediated translation in a circadian manner.
Kim et al., South Korea. In J Pineal Res, Nov 2015
Rhythmic arylalkylamine N-acetyltransferase (AANAT) synthesis is a prominent circadian-controlled response that occurs in most mammals.
Melatonin in the thyroid gland: regulation by thyroid-stimulating hormone and role in thyroglobulin gene expression.
Martin-Lacave et al., Sevilla, Spain. In J Physiol Pharmacol, Oct 2015
Our results show that the key enzymes for melatonin biosynthesis (AANAT and ASMT) are regulated by thyroid-stimulating hormone.
Experimental and clinical aspects of melatonin and clock genes in diabetes.
M├╝hlbauer et al., Leipzig, Germany. In J Pineal Res, Aug 2015
Melatonin levels in blood plasma, as well as the activity of the key enzyme of melatonin synthesis, AA-NAT (arylalkylamine-N-acetyltransferase) in pineal, are lower in type 2 diabetic rats compared to controls.
Melatonin in plants and other phototrophs: advances and gaps concerning the diversity of functions.
Hardeland, G├Âttingen, Germany. In J Exp Bot, Feb 2015
Serotonin N-acetyltransferase is localized in plastids and lacks homology to the vertebrate aralkylamine N-acetyltransferase. Melatonin content varies considerably among species, from a few picograms to several micrograms per gram, a strong hint for different actions of this indoleamine.
Gut Melatonin in Vertebrates: Chronobiology and Physiology.
Maitra et al., India. In Front Endocrinol (lausanne), 2014
Arylalkylamine N-acetyltransferase (AANAT) is the key regulator of its biosynthesis.
Fundamental issues related to the origin of melatonin and melatonin isomers during evolution: relation to their biological functions.
Reiter et al., San Antonio, United States. In Int J Mol Sci, 2013
Phylogenic analysis based on its rate-limiting synthetic enzyme, serotonin N-acetyltransferase (SNAT), indicates its multiple origins during evolution.
Homeobox genes and melatonin synthesis: regulatory roles of the cone-rod homeobox transcription factor in the rodent pineal gland.
Rath et al., Copenhagen, Denmark. In Biomed Res Int, 2013
Nocturnal synthesis of melatonin in the pineal gland is controlled by a circadian rhythm in arylalkylamine N-acetyltransferase (AANAT) enzyme activity.
Crystal structure of the dopamine N-acetyltransferase-acetyl-CoA complex provides insights into the catalytic mechanism.
Lyu et al., Taiwan. In Biochem J, 2012
Dat possesses a specialized active site structure dedicated to a catalytic mechanism.
MicroRNAs in the pineal gland: miR-483 regulates melatonin synthesis by targeting arylalkylamine N-acetyltransferase.
Klein et al., Bethesda, United States. In J Biol Chem, 2012
miR-483 suppresses Aanat mRNA levels during development and that the developmental decrease in miR-483 abundance promotes melatonin synthesis.
Melatonin exerts by an autocrine loop antiproliferative effects in cholangiocarcinoma: its synthesis is reduced favoring cholangiocarcinoma growth.
Alpini et al., Tempe, United States. In Am J Physiol Gastrointest Liver Physiol, 2011
There is dysregulation of the AANAT/ASMT/melatonin --> melatonin receptor axis in cholangiocarcinoma, which inhibited melatonin secretion and subsequently enhanced CCA growth.
Expression and cellular localizaion of melatonin-synthesizing enzymes in rat and human salivary glands.
Satomura et al., Yokohama, Japan. In Histochem Cell Biol, 2011
The expression of AANAT in epithelial cells of striated ducts in human submandibular glands.
Enhanced production of melatonin by ectopic overexpression of human serotonin N-acetyltransferase plays a role in cold resistance in transgenic rice seedlings.
Back et al., Kwangju, South Korea. In J Pineal Res, 2010
The functional expression of human SNA protein was closely associated with the elevated synthesis of N-acetylserotonin and melatonin in transgenic rice plants.
Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.
Dyda et al., Bethesda, United States. In Cell, 2001
Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin synthesis.
Correlates of sleep and waking in Drosophila melanogaster.
Tononi et al., San Diego, United States. In Science, 2000
Flies lacking one such enzyme, arylalkylamine N-acetyltransferase, show increased rest after rest deprivation.
The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.
Dyda et al., Bethesda, United States. In Cell, 1999
Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase superfamily, is the penultimate enzyme in the conversion of serotonin to melatonin, the circadian neurohormone.
Melatonin production: proteasomal proteolysis in serotonin N-acetyltransferase regulation.
Klein et al., Bethesda, United States. In Science, 1998
The nocturnal increase in circulating melatonin in vertebrates is regulated by 10- to 100-fold increases in pineal serotonin N-acetyltransferase (AA-NAT) activity.
Diurnal variation in mRNA encoding serotonin N-acetyltransferase in pineal gland.
Snyder et al., Baltimore, United States. In Nature, 1996
Serotonin N-acetyltransferase (NAT; EC2.3.1.87),
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