An enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine to N-acetylserotonin to form N-acetyl-5-methoxytryptamine (MELATONIN).
An enzyme that catalyzes the transfer of a methyl group from S-ADENOSYLMETHIONINE to the 5-position of CYTOSINE residues in DNA.
A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.
An enzyme that transfers methyl groups from O(6)-methylguanine, and other methylated moieties of DNA, to a cysteine residue in itself, thus repairing alkylated DNA in a single-step reaction. EC 2.1.1.63.
Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.
Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)
An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC 2.1.1.43.
Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.
Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs, primarily brain and spleen.
Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
Methylases that are specific for CYTOSINE residues found on DNA.
A PROTEIN O-METHYLTRANSFERASE that recognizes and catalyzes the methyl esterification of ISOASPARTIC ACID and D-ASPARTIC ACID residues in peptides and proteins. It initiates the repair of proteins damaged by the spontaneous decomposition of normal L-aspartic acid and L-asparagine residues.
Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the host-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognized by the restriction endonucleases of similar specificity and destroyed by cleavage. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms.
An enzyme responsible for producing a species-characteristic methylation pattern on adenine residues in a specific short base sequence in the host cell DNA. The enzyme catalyzes the methylation of DNA adenine in the presence of S-adenosyl-L-methionine to form DNA containing 6-methylaminopurine and S-adenosyl-L-homocysteine. EC 2.1.1.72.
Addition of methyl groups to DNA. DNA methyltransferases (DNA methylases) perform this reaction using S-ADENOSYLMETHIONINE as the methyl group donor.

The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog. (1/43)

Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase superfamily, is the penultimate enzyme in the conversion of serotonin to melatonin, the circadian neurohormone. Comparison of the structures of the substrate-free enzyme and the complex with a bisubstrate analog, coenzyme A-S-acetyltryptamine, demonstrates that acetyl coenzyme A (AcCoA) binding is accompanied by a large conformational change that in turn leads to the formation of the serotonin-binding site. The structure of the complex also provides insight into how the enzyme may facilitate acetyl transfer. A water-filled channel leading from the active site to the surface provides a pathway for proton removal following amine deprotonation. Furthermore, structural and mutagenesis results indicate an important role for Tyr-168 in catalysis.  (+info)

Melatonin, its precursors, and synthesizing enzyme activities in the human ovary. (2/43)

The presence of melatonin (N-acetyl-5-methoxytryptamine) and its precursors, serotonin (5-hydroxytryptamine) and N-acetylserotonin, was demonstrated in extracts of human ovary using reverse-phase high-performance liquid chromatography coupled with fluorometric detection. In addition, activities of two melatonin-synthesizing enzymes, arylalkylamine N-acetyltransferase (NAT) and hydroxyindole-O-methyltransferase (HIOMT), were found in human ovary homogenates. The apparent Michaelis constants for the substrates of NAT and HIOMT in the human ovary were similar to those reported for the pineal glands of humans and other mammals. These findings strongly suggest that the human ovary, like the pineal gland, may synthesize melatonin from serotonin by the sequential action of NAT and HIOMT.  (+info)

Genetic variability in plasma melatonin in sheep is due to pineal weight, not to variations in enzyme activities. (3/43)

This study was conducted to determine the origin of the high variability in the mean nocturnal plasma melatonin concentration (MC) in sheep. Two extreme groups of 25 lambs each [low (L) and high (H)] were obtained by calculating their genetic value on the basis of the MC of their parents. The MC of lambs was significantly higher in the H group than in the L group (L: 189.7 +/- 24.4 vs. H: 344.1 +/- 33.0 pg/ml, P < 0.001). Within each group, 13 lambs were slaughtered during the day (D) and 12 lambs during the night (N). Pineal weight was significantly higher in the H group than in the L group (L: 83.5 +/- 6.7 vs. H: 119.1 +/- 9.2 mg, P < 0.01) but did not differ between D and N. The amount of melatonin released in vitro per milligram of pineal gland, the arylalkylamine N-acetyltransferase (AANAT) activity, the AANAT protein content, and the level of AANAT mRNA differed significantly between D and N but not with genetic group. Hydroxyindole O-methyltransferase activity did not differ significantly between D and N or between genetic groups. Therefore, the genetic difference in MC between the two groups of lambs was attributed to a difference in pineal size, not in enzymatic activity of the pinealocytes.  (+info)

Identification of highly elevated levels of melatonin in bone marrow: its origin and significance. (4/43)

Bone marrow is an important tissue in generation of immunocompetent and peripheral blood cells. The progenitors of hematopoietic cells in bone marrow exhibit continuous proliferation and differentiation and they are highly vulnerable to acute or chronic oxidative stress. In this investigation, highly elevated levels of the antioxidant melatonin were identified in rat bone marrow using immunocytochemistry, radioimmunoassay, high performance liquid chromatography with electrochemical detection and mass spectrometry. Night-time melatonin concentrations (expressed as pg melatonin/mg protein) in the bone marrow of rats were roughly two orders of magnitude higher than those in peripheral blood. Measurement of the activities of the two enzymes (N-acetyltransferase (NAT) and hydroxyindole-O-methoxyltransferase (HIOMT)) which synthesize melatonin from serotonin showed that bone marrow cells have measurable NAT activity, but they have very low levels of HIOMT activity (at the one time they were measured). From these studies we could not definitively determine whether melatonin was produced in bone marrow cells or elsewhere. To investigate the potential pineal origin of bone marrow melatonin, long-term (8-month) pinealectomized rats were used to ascertain if the pineal gland is the primary source of this antioxidant. The bone marrow of pinealectomized rats, however, still exhibited high levels of melatonin. These results indicate that a major portion of the bone marrow's melatonin is of extrapineal origin. Immunocytochemistry clearly showed a positive melatonin reaction intracellularly in bone marrow cells. A melatonin concentrating mechanism in these cells is suggested by these findings and this may involve a specific melatonin binding protein. Since melatonin is an endogenous free radical scavenger and an immune-enhancing agent, the high levels of melatonin in bone marrow cells may provide on-site protection to reduce oxidative damage to these highly vulnerable hematopoietic cells and may enhance the immune capacity of cells such as lymphocytes.  (+info)

Regulation of hydroxyindole-O-methyltransferase gene expression in Japanese quail (Coturnix coturnix japonica). (5/43)

Hydroxyindole-O-methyltrasferase (HIOMT) plays an important role as the final enzyme in the synthesis of melatonin. In this study, the expression of the HIOMT gene in Japanese quail was investigated with respect to tissue distribution and the effects of light and vitamin A deficiency. HIOMT mRNA in the pineal gland and eye had a clear daily rhythm with peak values in daytime. The testis also contained a detectable amount of HIOMT mRNA, which did not display a rhythmic change over a 24-h period. When birds were rendered vitamin A deficient through feeding with a vitamin A-free diet, the daily rhythm of the HIOMT gene almost disappeared in both the pineal gland and eye due to increases in the nighttime values. Our previous observations and these results suggest that vitamin A and a photo-signal are required to maintain the rhythmic expression of the HIOMT gene as well as the arylalkylamine N-acetyltransferase gene.  (+info)

Conversion of L-tryptophan to serotonin and melatonin in human melanoma cells. (6/43)

We showed in human melanoma cells tryptophan hydroxylase (TPH) and hydroxyindole methyltransferase genes expression with the sequential enzymatic activities of TPH, serotonin (Ser) N-acetyltransferase and hydroxyindole methyltransferase. The presence of the products Ser, 5OH-tryptophan, N-acetylserotonin, melatonin (Mel), 5-methoxytryptamine and 5-methoxytryptophol was documented by liquid chromatography-mass spectrometry. Thus, human melanoma cells can synthesize and metabolize Ser and Mel.  (+info)

Serotoninergic and melatoninergic systems are fully expressed in human skin. (7/43)

We investigated the cutaneous expression of genes and enzymes responsible for the multistep conversion of tryptophan to serotonin and further to melatonin. Samples tested were human skin, normal and pathologic (basal cell carcinoma and melanoma), cultured normal epidermal and follicular melanocytes, melanoma cell lines, normal neonatal and adult epidermal and follicular keratinocytes, squamous cell carcinoma cells, and fibroblasts from dermis and follicular papilla. The majority of the samples showed simultaneous expression of the genes for tryptophan hydroxylase, arylalkylamine N-acetyltransferase (AANAT), and hydroxyindole-O-methyltransferase (HIOMT). The products of AANAT activity were identified by RP-HPLC with fluorimetric detection in human skin and in cultured normal and malignant melanocytes and immortalized keratinocytes; HIOMT activity was detected in human skin, keratinocytes, and melanoma cells. N-acetylserotonin (NAS) was detected by RP-HPLC in human skin extracts. NAS identity was confirmed further by LC/MS in keratinocytes. In conclusion, we provide evidence that the human skin expresses intrinsic serotonin and melatonin biosynthetic pathways.  (+info)

Molecular cloning and nucleotide sequence of a cDNA encoding hydroxyindole O-methyltransferase from chicken pineal gland. (8/43)

Hydroxyindole O-methyltransferase (EC 2.1.1.4) is the enzyme that catalyses the synthesis of melatonin in the pineal gland and in the retina. Polyadenylated RNA from chicken pineal glands was used to prepare a cDNA library in lambda gt11. The library was screened with an antiserum directed against chicken hydroxyindole O-methyltransferase, and one cDNA clone was isolated. The fusion protein expressed by phage lysogens was identified on Western blots as a 165 kDA immunoreactive protein (beta-galactosidase, 110 kDa; hydroxyindole O-methyltransferase, 38 kDa). The fusion protein exhibited hydroxyindole O-methyltransferase activity. Its Km values for N-acetyl-5-hydroxytryptamine and S-adenosylmethionine were 5 times those of the natural enzyme. The intrinsic activity of the fusion protein was approx. 0.25% that of the natural enzyme. The cDNA consisted of 1436 nucleotides, including a 1038-nucleotide sequence encoding a full-length 346-amino-acid hydroxyindole O-methyltransferase. Comparison with bovine hydroxyindole O-methyltransferase [Ishida, Obinata & Deguchi (1987) J. Biol. Chem. 262, 2895-2899] revealed 52% identity in nucleotide sequences and 44% identity in peptide sequences. Northern-blot analysis revealed the presence of hydroxyindole O-methyltransferase mRNA transcripts in chicken pineal gland and retina, but not in the telencephalon.  (+info)

Acetylserotonin O-methyltransferase (ASMT) is an enzyme that catalyzes the final step in melatonin synthesis. It transfers a methyl group from S-adenosylmethionine to acetylserotonin, forming melatonin and S-adenosylhomocysteine. ASMT plays a crucial role in regulating the sleep-wake cycle and other physiological processes influenced by melatonin.

Methyltransferases are a class of enzymes that catalyze the transfer of a methyl group (-CH3) from a donor molecule to an acceptor molecule, which is often a protein, DNA, or RNA. This transfer of a methyl group can modify the chemical and physical properties of the acceptor molecule, playing a crucial role in various cellular processes such as gene expression, signal transduction, and DNA repair.

In biochemistry, methyltransferases are classified based on the type of donor molecule they use for the transfer of the methyl group. The most common methyl donor is S-adenosylmethionine (SAM), a universal methyl group donor found in many organisms. Methyltransferases that utilize SAM as a cofactor are called SAM-dependent methyltransferases.

Abnormal regulation or function of methyltransferases has been implicated in several diseases, including cancer and neurological disorders. Therefore, understanding the structure, function, and regulation of these enzymes is essential for developing targeted therapies to treat these conditions.

Protein methyltransferases (PMTs) are a family of enzymes that transfer methyl groups from a donor, such as S-adenosylmethionine (SAM), to specific residues on protein substrates. This post-translational modification plays a crucial role in various cellular processes, including epigenetic regulation, signal transduction, and protein stability.

PMTs can methylate different amino acid residues, such as lysine, arginine, and histidine, on proteins. The methylation of these residues can lead to changes in the charge, hydrophobicity, or interaction properties of the target protein, thereby modulating its function.

For example, lysine methyltransferases (KMTs) are a subclass of PMTs that specifically methylate lysine residues on histone proteins, which are the core components of nucleosomes in chromatin. Histone methylation can either activate or repress gene transcription, depending on the specific residue and degree of methylation.

Protein arginine methyltransferases (PRMTs) are another subclass of PMTs that methylate arginine residues on various protein substrates, including histones, transcription factors, and RNA-binding proteins. Arginine methylation can also affect protein function by altering its interaction with other molecules or modulating its stability.

Overall, protein methyltransferases are essential regulators of cellular processes and have been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the mechanisms and functions of PMTs is crucial for developing novel therapeutic strategies to target these diseases.

Methylation, in the context of genetics and epigenetics, refers to the addition of a methyl group (CH3) to a molecule, usually to the nitrogenous base of DNA or to the side chain of amino acids in proteins. In DNA methylation, this process typically occurs at the 5-carbon position of cytosine residues that precede guanine residues (CpG sites) and is catalyzed by enzymes called DNA methyltransferases (DNMTs).

DNA methylation plays a crucial role in regulating gene expression, genomic imprinting, X-chromosome inactivation, and suppression of repetitive elements. Hypermethylation or hypomethylation of specific genes can lead to altered gene expression patterns, which have been associated with various human diseases, including cancer.

In summary, methylation is a fundamental epigenetic modification that influences genomic stability, gene regulation, and cellular function by introducing methyl groups to DNA or proteins.

Histone-Lysine N-Methyltransferase is a type of enzyme that transfers methyl groups to specific lysine residues on histone proteins. These histone proteins are the main protein components of chromatin, which is the complex of DNA and proteins that make up chromosomes.

Histone-Lysine N-Methyltransferases play a crucial role in the regulation of gene expression by modifying the structure of chromatin. The addition of methyl groups to histones can result in either the activation or repression of gene transcription, depending on the specific location and number of methyl groups added.

These enzymes are important targets for drug development, as their dysregulation has been implicated in various diseases, including cancer. Inhibitors of Histone-Lysine N-Methyltransferases have shown promise in preclinical studies for the treatment of certain types of cancer.

tRNA (transfer RNA) methyltransferases are a group of enzymes that catalyze the transfer of a methyl group (-CH3) to specific positions on the tRNA molecule. These enzymes play a crucial role in modifying and regulating tRNA function, stability, and interaction with other components of the translation machinery during protein synthesis.

The addition of methyl groups to tRNAs can occur at various sites, including the base moieties of nucleotides within the anticodon loop, the TψC loop, and the variable region. These modifications help maintain the structural integrity of tRNA molecules, enhance their ability to recognize specific codons during translation, and protect them from degradation by cellular nucleases.

tRNA methyltransferases are classified based on the type of methylation they catalyze:

1. N1-methyladenosine (m1A) methyltransferases: These enzymes add a methyl group to the N1 position of adenosine residues in tRNAs. An example is TRMT6/TRMT61A, which methylates adenosines at position 58 in human tRNAs.
2. N3-methylcytosine (m3C) methyltransferases: These enzymes add a methyl group to the N3 position of cytosine residues in tRNAs. An example is Dnmt2, which methylates cytosines at position 38 in various organisms.
3. N7-methylguanosine (m7G) methyltransferases: These enzymes add a methyl group to the N7 position of guanosine residues in tRNAs, primarily at position 46 within the TψC loop. An example is Trm8/Trm82, which catalyzes this modification in yeast and humans.
4. 2'-O-methylated nucleotides (Nm) methyltransferases: These enzymes add a methyl group to the 2'-hydroxyl group of ribose sugars in tRNAs, which can occur at various positions throughout the molecule. An example is FTSJ1, which methylates uridines at position 8 in human tRNAs.
5. Pseudouridine (Ψ) synthases: Although not technically methyltransferases, pseudouridine synthases catalyze the isomerization of uridine to pseudouridine, which can enhance tRNA stability and function. An example is Dyskerin (DKC1), which introduces Ψ at various positions in human tRNAs.

These enzymes play crucial roles in modifying tRNAs, ensuring proper folding, stability, and function during translation. Defects in these enzymes can lead to various diseases, including neurological disorders, cancer, and premature aging.

Protein-Arginine N-Methyltransferases (PRMTs) are a group of enzymes that catalyze the transfer of methyl groups from S-adenosylmethionine to specific arginine residues in proteins, leading to the formation of N-methylarginines. This post-translational modification plays a crucial role in various cellular processes such as signal transduction, DNA repair, and RNA processing. There are nine known PRMTs in humans, which can be classified into three types based on the type of methylarginine produced: Type I (PRMT1, 2, 3, 4, 6, and 8) produce asymmetric dimethylarginines, Type II (PRMT5 and 9) produce symmetric dimethylarginines, and Type III (PRMT7) produces monomethylarginine. Aberrant PRMT activity has been implicated in several diseases, including cancer and neurological disorders.

S-Adenosylmethionine (SAMe) is a physiological compound involved in methylation reactions, transulfuration pathways, and aminopropylation processes in the body. It is formed from the coupling of methionine, an essential sulfur-containing amino acid, and adenosine triphosphate (ATP) through the action of methionine adenosyltransferase enzymes.

SAMe serves as a major methyl donor in various biochemical reactions, contributing to the synthesis of numerous compounds such as neurotransmitters, proteins, phospholipids, nucleic acids, and other methylated metabolites. Additionally, SAMe plays a crucial role in the detoxification process within the liver by participating in glutathione production, which is an important antioxidant and detoxifying agent.

In clinical settings, SAMe supplementation has been explored as a potential therapeutic intervention for various conditions, including depression, osteoarthritis, liver diseases, and fibromyalgia, among others. However, its efficacy remains a subject of ongoing research and debate within the medical community.

DNA cytosine methylases are a type of enzyme that catalyze the transfer of a methyl group (-CH3) to the carbon-5 position of the cytosine ring in DNA, forming 5-methylcytosine. This process is known as DNA methylation and plays an important role in regulating gene expression, genomic imprinting, X-chromosome inactivation, and suppression of transposable elements in eukaryotic organisms.

In mammals, the most well-studied DNA cytosine methylases are members of the DNMT (DNA methyltransferase) family, including DNMT1, DNMT3A, and DNMT3B. DNMT1 is primarily responsible for maintaining existing methylation patterns during DNA replication, while DNMT3A and DNMT3B are involved in establishing new methylation patterns during development and differentiation.

Abnormal DNA methylation patterns have been implicated in various diseases, including cancer, where global hypomethylation and promoter-specific hypermethylation can contribute to genomic instability, chromosomal aberrations, and silencing of tumor suppressor genes.

Protein D-aspartate-L-isoaspartate methyltransferase (PCMT or PRMT5) is an enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine to the side chain nitrogen atom of a specific aspartate or glutamate residue on protein substrates. This enzyme plays a crucial role in the maintenance of protein structure and function by correcting the spontaneous deamidation of asparagine and isomerization of aspartate to isoaspartate residues, which can lead to protein aggregation and loss of function. PCMT also regulates various cellular processes, including transcription, RNA processing, DNA damage repair, and signal transduction, by modifying the activity or localization of its target proteins.

DNA modification methylases are a type of enzyme that catalyze the transfer of methyl groups (-CH3) to specific nucleotides in DNA, usually cytosine or adenine residues. This process is known as DNA methylation and is an important epigenetic mechanism that regulates gene expression, genome stability, and other cellular processes.

There are several types of DNA modification methylases, including:

1. Cytosine-5 methyltransferases (CNMTs or DNMTs): These enzymes catalyze the transfer of a methyl group to the fifth carbon atom of cytosine residues in DNA, forming 5-methylcytosine (5mC). This is the most common type of DNA methylation and plays a crucial role in gene silencing, X-chromosome inactivation, and genomic imprinting.
2. N6-adenine methyltransferases (MTases): These enzymes catalyze the transfer of a methyl group to the sixth nitrogen atom of adenine residues in DNA, forming N6-methyladenine (6mA). This type of DNA methylation is less common than 5mC but has been found to be involved in various cellular processes, such as transcriptional regulation and DNA repair.
3. GpC methyltransferases: These enzymes catalyze the transfer of a methyl group to the second carbon atom of guanine residues in DNA, forming N4-methylcytosine (4mC). This type of DNA methylation is relatively rare and has been found mainly in prokaryotic genomes.

Dysregulation of DNA modification methylases has been implicated in various diseases, including cancer, neurological disorders, and immunological diseases. Therefore, understanding the function and regulation of these enzymes is essential for developing novel therapeutic strategies to treat these conditions.

DNA methylation is a process by which methyl groups (-CH3) are added to the cytosine ring of DNA molecules, often at the 5' position of cytospine phosphate-deoxyguanosine (CpG) dinucleotides. This modification is catalyzed by DNA methyltransferase enzymes and results in the formation of 5-methylcytosine.

DNA methylation plays a crucial role in the regulation of gene expression, genomic imprinting, X chromosome inactivation, and suppression of transposable elements. Abnormal DNA methylation patterns have been associated with various diseases, including cancer, where tumor suppressor genes are often silenced by promoter methylation.

In summary, DNA methylation is a fundamental epigenetic modification that influences gene expression and genome stability, and its dysregulation has important implications for human health and disease.

... (ASMT), Acetylserotonin N-methyltransferase, Acetylserotonin methyltransferase (Y ... Acetylserotonin O-methyltransferase has been determined by X-ray diffraction. N-Acetylserotonin O-methyltransferase can be ... Acetylserotonin O-methyltransferase The second reaction (Figure 4) catalyzed by N-Acetylserotonin O-methyltransferase in the ... Synonyms of N- Acetylserotonin O-methyltransferase are Hydroxyindole O-methyltransferase (HIOMT), ...
... is an enzyme that in humans is encoded by the ASMTL gene. GRCh38: Ensembl ... "Entrez Gene: ASMTL acetylserotonin O-methyltransferase-like". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to ... Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein) at the PDBe-KB. v t e (Articles with short ...
Hydroxyindole O-methyltransferase and S-adenosyl methionine convert N-acetylserotonin into melatonin through methylation of the ... N-Acetylserotonin is methylated at the hydroxyl position by S-adenosyl methionine (SAM) to produce S-adenosyl homocysteine (SAH ... The thiol from coenzyme A serves as a good leaving group when attacked by a general base to give N-acetylserotonin. ... Donohue SJ, Roseboom PH, Illnerova H, Weller JL, Klein DC (October 1993). "Human hydroxyindole-O-methyltransferase: presence of ...
N-acetylserotonin is converted into melatonin by the enzyme hydroxyindole O-methyltransferase (HIOMT), also known as ... acetylserotonin O-methyltransferase (ASMT). Activity of these enzymes is high during the night and regulated by the mechanisms ... The serotonin is then acetylated by the AANAT enzyme and converted into N-acetylserotonin. ...
N-acetylserotonin O-methyltransferase (ASMT) to generate melatonin. The N-acetyltransferase reaction has been suggested to be ... After the transfer of the acetyl group has occurred, the products are orderly released with N-acetyl-serotonin first and CoA ... In the biosynthesis of melatonin, N-acetylserotonin is further methylated by another enzyme, ... to produce N-acetylserotonin. Based on this mechanism, it might be expected that a bisubstrate analog inhibitor, derived from ...
... and is converted to melatonin by acetylserotonin O-methyltransferase (ASMT). NAS is able to penetrate the blood-brain barrier, ... "N-Acetyl Serotonin". DrugBank. (CS1 Russian-language sources (ru), Articles without KEGG source, ECHA InfoCard ID from Wikidata ... 1999). "N-acetylserotonin is a better extra- and intracellular antioxidant than melatonin". FEBS Lett. 449 (2-3): 206-10. doi: ... February 2010). "N-acetylserotonin activates TrkB receptor in a circadian rhythm". Proceedings of the National Academy of ...
Examples are : Acetylserotonin O-methyltransferase Apigenin 4'-O-methyltransferase Caffeate O-methyltransferase Caffeoyl-CoA O- ... O-methyltransferase Kaempferol 4'-O-methyltransferase Licodione 2'-O-methyltransferase Loganate O-methyltransferase Luteolin O- ... O-methyltransferase Phenol O-methyltransferase Polysaccharide O-methyltransferase Protein-glutamate O-methyltransferase Protein ... methyltransferase Catechol O-methyltransferase Chlorophenol O-methyltransferase Columbamine O-methyltransferase ...
... thetin-homocysteine S-methyltransferase EC 2.1.1.4: acetylserotonin O-methyltransferase EC 2.1.1.5: betaine-homocysteine S- ... methyltransferase EC 2.1.1.6: catechol O-methyltransferase EC 2.1.1.7: nicotinate N-methyltransferase EC 2.1.1.8: histamine N- ... phenol O-methyltransferase EC 2.1.1.26: iodophenol O-methyltransferase EC 2.1.1.27: tyramine N-methyltransferase EC 2.1.1.28: ... inositol 1-methyltransferase EC 2.1.1.41: sterol 24-C-methyltransferase EC 2.1.1.42: flavone 3′-O-methyltransferase EC 2.1.1.43 ...
... methyltransferases MeSH D08.811.913.555.500.100 - acetylserotonin n-methyltransferase MeSH D08.811.913.555.500.175 - betaine- ... histone-lysine n-methyltransferase MeSH D08.811.913.555.500.800.650 - o-6-methylguanine-DNA methyltransferase MeSH D08.811. ... protein o-methyltransferase MeSH D08.811.913.555.500.800.800.700 - protein d-aspartate-l-isoaspartate methyltransferase MeSH ... homocysteine S-methyltransferase MeSH D08.811.913.555.500.250 - catechol O-methyltransferase MeSH D08.811.913.555.500.350 - dna ...
As of 2000, a number of genes were known to be Y-linked, including: ASMTY (acetylserotonin methyltransferase), TSPY (testis- ...
... is known to act as a histamine N-methyltransferase inhibitor. This explains how harmaline elicits its wakefulness- ... Harmaline forces the anabolic metabolism of serotonin into N-acetylserotonin (normelatonin), and then to melatonin, the body's ... Cumming P, Vincent SR (September 1992). "Inhibition of histamine-N-methyltransferase (HNMT) by fragments of 9-amino-1,2,3,4- ...
In addition to the main metabolic pathway, TAs can also be converted by nonspecific N-methyltransferase (NMT) [22] and ... Other biogenic monoamines Trimethylamine Trimethylamine N-oxide Indoleamines Melatonin 6-Hydroxymelatonin N-Acetylserotonin ... phenylethanolamine N-methyltransferase (PNMT) [23] to the corresponding secondary amines (e.g. synephrine [14], N- ...
Acetylserotonin O-methyltransferase (ASMT), Acetylserotonin N-methyltransferase, Acetylserotonin methyltransferase (Y ... Acetylserotonin O-methyltransferase has been determined by X-ray diffraction. N-Acetylserotonin O-methyltransferase can be ... Acetylserotonin O-methyltransferase The second reaction (Figure 4) catalyzed by N-Acetylserotonin O-methyltransferase in the ... Synonyms of N- Acetylserotonin O-methyltransferase are Hydroxyindole O-methyltransferase (HIOMT), ...
Substrates→Products: Serotonin→N-Acetylserotonin. ASMTTooltip Acetylserotonin O-methyltransferase. *Substrates→Products: N- ... Catechol-O-methyltransferase is shown in green boxes.[5][6]. Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several ... 2010). Basic Aspects of Catechol-O-Methyltransferase and the Clinical Applications of its Inhibitors. Academic Press. p. 34. ... Tai CH, Wu RM (February 2002). "catechol-O-methyltransferase and Parkinsons disease". Acta Medica Okayama. 56 (1): 1-6. doi: ...
Acetylserotonin N-Methyltransferase. Acetylserotonin O-Methyltransferase. Ca(2+)-Calmodulin Dependent Protein Kinase. Calcium- ...
Acetylserotonin N-Methyltransferase. Acetylserotonin O-Methyltransferase. Ca(2+)-Calmodulin Dependent Protein Kinase. Calcium- ...
Acetylserotonin methyltransferase (ASMT) catalyzed the final enzymatic reaction in melatonin production. Melatonin accumulation ... We report that methyltransferase SMYD2 plays an essential role in nonhomologous end joining repair (NHEJ), driving tumor cells ...
N-acetylserotonin O-methyltransferase (ASMT, HIOMT synonym) to generate melatonin. The ASMT final reaction has been suggested ... Maternal and placental MT provides protection against DNA damage, including by the inhibition of DNA methyltransferase [59][27] ... thereby producing CoA and N-acetylserotonin (NAS). In the biosynthesis of melatonin, NAS is further methylated by another ...
... acetylserotonin-O-methyltransferase (ASMT, OMIM *300015), is implicated as a susceptibility gene for ASD [82]. ...
N-acetylserotonin methyltransferase (ASMT), in the wheat drought response-gene network. Promoter analysis of the ASMT gene ... namely O-METHYLTRANSFERASE 1 (OMT1). Accordingly, molecular and physiochemical evaluations were performed in a separate ...
Human ASMT(Acetylserotonin-O-Methyltransferase) ELISA Kit. *Human ASNS(Asparagine Synthetase) ELISA Kit ...
Human ASMT(Acetylserotonin-O-Methyltransferase) ELISA Kit. *Human ASNS(Asparagine Synthetase) ELISA Kit ...
Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is Strongly Expressed in a Subpopulation of Pinealocytes in the ... Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is Strongly Expressed in a Subpopulation of Pinealocytes in the ... Acetylserotonin O-Methyltransferase), and Aanat (Aralkylamine N-Acetyltransferase) mRNA Expressions in Rat Testes. Coelho LA, ... acetylserotonin O-methyltransferase (ASMT), and in situ hybridization techniques to study transcripts encoding ASMT and two ...
Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is Strongly Expressed in a Subpopulation of Pinealocytes in the ... Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is Strongly Expressed in a Subpopulation of Pinealocytes in the ... Acetylserotonin O-Methyltransferase), and Aanat (Aralkylamine N-Acetyltransferase) mRNA Expressions in Rat Testes. Coelho LA, ... acetylserotonin O-methyltransferase (ASMT), and in situ hybridization techniques to study transcripts encoding ASMT and two ...
Acetylserotonin N-Methyltransferase. Acetylserotonin O-Methyltransferase. Ca(2+)-Calmodulin Dependent Protein Kinase. Calcium- ...
A Comparative Genomic and Transcriptomic Survey Provides Novel Insights into N-Acetylserotonin Methyltransferase (ASMT) in Fish ...
Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is Strongly Expressed in a Subpopulation of Pinealocytes in the ... 2. Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell ...
Molecular docking studies for the identification of novel melatoninergic inhibitors for acetylserotonin-O-methyltransferase ...
More about Acetylserotonin O-Methyltransferase. Subject Term Type Topical. Acetylserotonin O-Methyltransferase. ...
Acetylserotonin methyltransferase (substance). Code System Preferred Concept Name. Acetylserotonin methyltransferase (substance ... Substance with methyltransferase mechanism of action (substance) {130055001 , SNOMED-CT } Substance with transferase mechanism ...
... see ACETYLSEROTONIN N-METHYLTRANSFERASE 1998-2007, see ACETYLSEROTONIN METHYLTRANSFERASE 1991-1997, see METHYLTRANSFERASES 1975 ... Acetylserotonin Methyltransferase HIOMT Hydroxyindole O-Methyltransferase Oxyindol-O-Methyltransferase Registry Number. EC 2.1. ... Methyltransferases [D08.811.913.555.500] * Acetylserotonin O-Methyltransferase [D08.811.913.555.500.100] * Betaine-Homocysteine ... S-Adenosyl-L-methionine:N-acetylserotonin O-methyltransferase. Previous Indexing. Methyltransferases (1974). Serotonin (1974). ...
... see ACETYLSEROTONIN N-METHYLTRANSFERASE 1998-2007, see ACETYLSEROTONIN METHYLTRANSFERASE 1991-1997, see METHYLTRANSFERASES 1975 ... Acetylserotonin Methyltransferase HIOMT Hydroxyindole O-Methyltransferase Oxyindol-O-Methyltransferase Registry Number. EC 2.1. ... Methyltransferases [D08.811.913.555.500] * Acetylserotonin O-Methyltransferase [D08.811.913.555.500.100] * Betaine-Homocysteine ... S-Adenosyl-L-methionine:N-acetylserotonin O-methyltransferase. Previous Indexing. Methyltransferases (1974). Serotonin (1974). ...
GO:0008171: O-methyltransferase activity GO:0042802: identical protein binding GO:0017096: acetylserotonin O-methyltransferase ...
N-Acetylserotonin is then O-methylated by hydroxyindole O-methyltransferase to form melatonin, S-adenosylmethio- nine serving ... N-acetylserotonin; HIAA, 5-hydroxyin- doleacetic acid; HIOMT, hydroxyindole O-methyltransferase; and NA, noradrena- line. ... mone melatonin then follows as a result of O-methylation of N-acetylserotonin by hydroxyindole O-methyltransferase. The ... Thus, the rise in N-acetyltratis- ferase at night causes a fall in sero- tonin and a rise in N-acetylserotonin, the precursor ...
Acetylserotonin N-Methyltransferase. Acetylserotonin O-Methyltransferase. Ca(2+)-Calmodulin Dependent Protein Kinase. Calcium- ...
... while the C-terminus is similar to N-acetylserotonin O-methyltransferase. This gene is located in the pseudoautosomal region 1 ... The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity. The ... N-acetylserotonin O-methyltransferase-like Protein. DTO Classes. Protein. / Enzyme. / Transferase. / Methyltransferase. / N- ... while the C-terminus is similar to N-acetylserotonin O-methyltransferase. This gene is located in the pseudoautosomal region 1 ...
... while the C-terminus is similar to N-acetylserotonin O-methyltransferase. This gene is located in the pseudoautosomal region 1 ... The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity. The ... N-acetylserotonin O-methyltransferase-like Protein. DTO Classes. Protein. / Enzyme. / Transferase. / Methyltransferase. / N- ... while the C-terminus is similar to N-acetylserotonin O-methyltransferase. This gene is located in the pseudoautosomal region 1 ...
Isoglutamine N0000168195 Acetylserotonin N-Methyltransferase N0000178559 Acetylserotonin O-Methyltransferase N0000166506 ... Kinase C-epsilon N0000168228 Protein Kinases N0000168182 Protein Methyltransferases N0000168184 Protein O-Methyltransferase ... Methyltransferase N0000170655 DNA Adducts N0000168002 DNA Glycosylases N0000168107 DNA Gyrase N0000168096 DNA Helicases ... Methylguanine-DNA Methyltransferase N0000170815 O-Acetyl-ADP-Ribose N0000166306 o-Aminoazotoluene N0000166570 o- ...
Acetylserotonin O-Methyltransferase. Genre(s):. Archival Materials. Articles. Abstract:. In this brief article, Axelrod and ... Enzymatic O-Methylation of N-Acetylserotonin to Melatonin. Contributor(s):. Axelrod, Julius, 1912-2004. Science. Weissbach, ... Weissbach reported their isolation of an enzyme, hydroxyindole-O-methyl transferase (HIOMT), which plays a key role in the ...
Acetylserotonin O-Methyltransferase), and Aanat (Aralkylamine N-Acetyltransferase) mRNA Expressions in Rat Testes. Molecular ...
N-acetylserotonin methyltransferase (ASMT), in the wheat drought response-gene network. Promoter analysis of the ASMT gene ... Among those genes, O-methyl transferase 1 (OMT1) was highlighted as a more important (hub) gene in the dual-stress response ... O-methyl transferase 1 (OMT1) and wheat (Triticum aestivum L.) combined drought and salinity stress tolerance. Shamloo- ... O-methyl transferase 1 (OMT1) and wheat (Triticum aestivum L.) combined drought and salinity stress tolerance. Planta, 255(5), ...
Acetylserotonin N-Methyltransferase [] MH NEW = Acetylserotonin O-Methyltransferase MH OLD = Addresses [Publication Type] [] MH ...
Human ASMT(Acetylserotonin-O-Methyltransferase) ELISA Kit. *Human ASNS(Asparagine Synthetase) ELISA Kit ...
Human ASMT(Acetylserotonin-O-Methyltransferase) ELISA Kit. *Human ASNS(Asparagine Synthetase) ELISA Kit ...
Acetylserotonin Methyltransferase Acetylserotonin N Methyltransferase,Acetylserotonin N Methyltransferase Acetylserotonin N- ... Methyltransferase,Acetylserotonin N-Methyltransferase Acetylserotonin methyltransferase,Acetylserotonin methyltransferase Ache ... N-acetylserotonin O-methyltransferase,S-Adenosyl-L-methionine:N-acetylserotonin O-methyltransferase SCC-Squam cell carcin of ...
  • N-Acetylserotonin O-methyltransferase, also known as ASMT, is an enzyme which catalyzes the final reaction in melatonin biosynthesis: converting Normelatonin to melatonin. (wikipedia.org)
  • Synonyms of N- Acetylserotonin O-methyltransferase are Hydroxyindole O-methyltransferase (HIOMT), Acetylserotonin O-methyltransferase (ASMT), Acetylserotonin N-methyltransferase, Acetylserotonin methyltransferase (Y chromosome). (wikipedia.org)
  • In the biosynthesis of melatonin, NAS is further methylated by another enzyme, N-acetylserotonin O-methyltransferase (ASMT, HIOMT synonym) to generate melatonin. (encyclopedia.pub)
  • One specific correlate of ASD is a low level of melatonin, and one of the enzymes critical in the synthesis of melatonin, acetylserotonin-O-methyltransferase (ASMT, OMIM *300015), is implicated as a susceptibility gene for ASD [82]. (the-mouse-trap.com)
  • The most commonly used synonym is Hydroxyindole O-methyltransferase (HIOMT). (wikipedia.org)
  • Figure 4: Second reaction catalyzed by N- Acetylserotonin O-methyltransferase Figure 5 is a more general scheme of the reaction pathway from serotonin to melatonin. (wikipedia.org)
  • This finding, in conjunction with research on alternative splicing of the HOIMT hnRNA, suggests that Hydroxyindole O-methyltransferase (synonym for N- Acetylserotonin O-methyltransferase) plays a role in the human immune system, in addition to its endocrine and nervous system functions. (wikipedia.org)
  • The other enzyme which catalyzes this reaction is n-acetylserotonin-o-methyltransferase-like-protein. (wikipedia.org)
  • N-Acetylserotonin O-methyltransferase is an enzyme that is coded for by genes located on the pseudoautosomal region of the X and Y chromosome, and is most abundantly found in the pineal gland and retina of humans. (wikipedia.org)
  • N-Acetylserotonin O-methyltransferase can be classified under three types of enzyme functional groups: transferases, one-carbon group transferrers, and methyltransferases. (wikipedia.org)
  • Serotonin has many fates in this pathway, and N- Acetylserotonin O-methyltransferase catalyzes reactions in two of these fates. (wikipedia.org)
  • AANAT catalyzes the transfer of the acetyl group of Acetyl-CoA to the primary amine of serotonin, thereby producing CoA and N-acetylserotonin (NAS). (encyclopedia.pub)
  • [7] In humans, catechol- O -methyltransferase protein is encoded by the COMT gene . (wikipedia.org)
  • A functional single-nucleotide polymorphism (a common normal variant) of the gene for catechol- O -methyltransferase results in a valine to methionine mutation at position 158 (Val 158 Met) rs4680 . (wikipedia.org)
  • The structure of N- Acetylserotonin O-methyltransferase has been determined by X-ray diffraction. (wikipedia.org)
  • Catechol- O -methyltransferase is shown in green boxes. (wikipedia.org)
  • 2. Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors. (nih.gov)
  • N-Acetylserotonin is then O-methylated by hydroxyindole O-methyltransferase to form melatonin, S-adenosylmethio- nine serving as the methyl donor (/5). (nih.gov)
  • Hydroxyindole O-methyltransferase is highly. (nih.gov)
  • The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity. (nih.gov)
  • In other classes (rep- tiles, amphibia, and fish), hydroxy- indole O-methyltransferase is also found in 'the eye and brain as well as the pineal region (J6). (nih.gov)