AS3MT

Last updated
AS3MT
Identifiers
Aliases AS3MT , CYT19, arsenite methyltransferase
External IDs OMIM: 611806 MGI: 1929882 HomoloGene: 10754 GeneCards: AS3MT
Gene location (Human)
Ideogram human chromosome 10.svg
Chr. Chromosome 10 (human) [1]
Human chromosome 10 ideogram.svg
HSR 1996 II 3.5e.svg
Red rectangle 2x18.png
Band 10q24.32Start102,869,470 bp [1]
End102,901,899 bp [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_020682

NM_020577

RefSeq (protein)

NP_065733

NP_065602

Location (UCSC) Chr 10: 102.87 – 102.9 Mb Chr 19: 46.71 – 46.74 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Arsenite methyltransferase is an enzyme that in humans is encoded by the AS3MT gene. [5] [6]

Contents

Related Research Articles

Arsenic poisoning is a medical condition that occurs due to elevated levels of arsenic in the body. If arsenic poisoning occurs over a brief period of time, symptoms may include vomiting, abdominal pain, encephalopathy, and watery diarrhea that contains blood. Long-term exposure can result in thickening of the skin, darker skin, abdominal pain, diarrhea, heart disease, numbness, and cancer.

Catechol-<i>O</i>-methyltransferase

Catechol-O-methyltransferase is one of several enzymes that degrade catecholamines, catecholestrogens, and various drugs and substances having a catechol structure. In humans, catechol-O-methyltransferase protein is encoded by the COMT gene. Two isoforms of COMT are produced: the soluble short form (S-COMT) and the membrane bound long form (MB-COMT). As the regulation of catecholamines is impaired in a number of medical conditions, several pharmaceutical drugs target COMT to alter its activity and therefore the availability of catecholamines. COMT was first discovered by the biochemist Julius Axelrod in 1957.

Toxicogenomics is a subdiscipline of pharmacology that deals with the collection, interpretation, and storage of information about gene and protein activity within a particular cell or tissue of an organism in response to exposure to toxic substances. Toxicogenomics combines toxicology with genomics or other high-throughput molecular profiling technologies such as transcriptomics, proteomics and metabolomics. Toxicogenomics endeavors to elucidate the molecular mechanisms evolved in the expression of toxicity, and to derive molecular expression patterns that predict toxicity or the genetic susceptibility to it.

CYP2A6

Cytochrome P450 2A6 is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. CYP2A6 is the primary enzyme responsible for the oxidation of nicotine and cotinine. It is also involved in the metabolism of several pharmaceuticals, carcinogens, and a number of coumarin-type alkaloids. CYP2A6 is the only enzyme in the human body that appreciably catalyzes the 7-hydroxylation of coumarin, such that the formation of the product of this reaction, 7-hydroxycoumarin, is used as a probe for CYP2A6 activity.

Thiopurine methyltransferase

Thiopurine methyltransferase or thiopurine S-methyltransferase (TPMT) is an enzyme that in humans is encoded by the TPMT gene. A pseudogene for this locus is located on chromosome 18q.

CYP1A1 Protein-coding gene in the species Homo sapiens

Cytochrome P450, family 1, subfamily A, polypeptide 1 is a protein that in humans is encoded by the CYP1A1 gene. The protein is a member of the cytochrome P450 superfamily of enzymes.

CYP2B6

Cytochrome P450 2B6 is an enzyme that in humans is encoded by the CYP2B6 gene. CYP2B6 is a member of the cytochrome P450 group of enzymes. Along with CYP2A6, it is involved with metabolizing nicotine, along with many other substances.

Acetylserotonin O-methyltransferase

N-Acetylserotonin O-methyltransferase, also known as ASMT, is an enzyme which catalyzes the final reaction in melatonin biosynthesis: converting Normelatonin to melatonin. This reaction is embedded in the more general tryptophan metabolism pathway. The enzyme also catalyzes a second reaction in tryptophan metabolism: the conversion of 5-hydroxy-indoleacetate to 5-methoxy-indoleacetate. The other enzyme which catalyzes this reaction is n-acetylserotonin-o-methyltransferase-like-protein.

Phosphatidylethanolamine N-methyltransferase

Phosphatidylethanolamine N-methyltransferase is a transferase enzyme which converts phosphatidylethanolamine (PE) to phosphatidylcholine (PC) in the liver. In humans it is encoded by the PEMT gene within the Smith–Magenis syndrome region on chromosome 17.

PON1

Serum paraoxonase and arylesterase 1 (PON1) also known as A esterase , homocysteine thiolactonase or serum aryldialkylphosphatase 1 is an enzyme that in humans is encoded by the PON1 gene. Paraoxonase 1 has esterase and more specifically paraoxonase activity. Serum PON1 is found in all mammalian species studied so far but is not present in the serum of birds, fish and reptiles or in insects. PON1 is the first discovered member of a multigene family also containing PON2 and PON3, the genes for which are located adjacent to each other on chromosome 7.

Flavin containing monooxygenase 1 Protein-coding gene in the species Homo sapiens

Dimethylaniline monooxygenase [N-oxide-forming] 1 is an enzyme that in humans is encoded by the FMO1 gene.

SULT1A2

Sulfotransferase 1A2 is an enzyme that in humans is encoded by the SULT1A2 gene.

GNMT

Glycine N-methyltransferase is an enzyme that in humans is encoded by the GNMT gene.

HTR3B

5-hydroxytryptamine (serotonin) receptor 3B, also known as HTR3B, is a human gene. The protein encoded by this gene is a subunit of the 5-HT3 receptor.

ALDH1A1

Aldehyde dehydrogenase 1 family, member A1, also known as ALDH1A1 or retinaldehyde dehydrogenase 1 (RALDH1), is an enzyme that in humans is encoded by the ALDH1A1 gene.

Arsenic biochemistry refers to biochemical processes that can use arsenic or its compounds, such as arsenate. Arsenic is a moderately abundant element in Earth's crust, and although many arsenic compounds are often considered highly toxic to most life, a wide variety of organoarsenic compounds are produced biologically and various organic and inorganic arsenic compounds are metabolized by numerous organisms. This pattern is general for other related elements, including selenium, which can exhibit both beneficial and deleterious effects. Arsenic biochemistry has become topical since many toxic arsenic compounds are found in some aquifers, potentially affecting many millions of people via biochemical processes.

Arsenite methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:arsenite As-methyltransferase. This enzyme catalyses the following chemical reaction

KIF6

Kinesin family member 6 is a protein that in humans is encoded by the KIF6 gene. This gene encodes a member of the kinesin family of proteins. Members of this family are part of a multisubunit complex that functions as a microtubule motor in intracellular organelle transport.

Karin Broberg is a Swedish geneticist and toxicologist and professor at Karolinska Institutet, Sweden, known for her work on human adaptation to challenging environments. Based on knowledge gained from expeditions to remote Andean plains with high arsenic in drinking waters, she observed that indigenous populations of Indians inhabiting these areas since thousands of years are naturally resistant to arsenic., which is a highly toxic chemical. Arsenic tolerance was in resistant individuals found to be the result of allelic variation in the arsenic-3-methyl transferase (AS3MT) gene, the gene product of which detoxifies arsenic. This was the first report on human genetic adaptation to a toxic environment and added to the list of very few examples of evolution of humans in historic time. Her subsequent work has provided phylogenetic evidence that the AS3MT gene moved by horizontal gene transfer from bacteria to animals during their early evolution, and independently on several occasions to other eukaryotic phylae as well. Horizontal gene transfer is distinct from vertical gene transfer from progeny to progeny, as such transfer of single genes as a means of obtaining new stably inherited trait has only rarely been reported in animals

N6AMT1

N-6 adenine-specific DNA methyltransferase 1 is a protein that in humans is encoded by the N6AMT1 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000214435 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000003559 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL, Simeonsson JB, Thomas DJ (March 2002). "A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol". The Journal of Biological Chemistry. 277 (13): 10795–803. doi: 10.1074/jbc.M110246200 . PMID   11790780.
  6. "Entrez Gene: AS3MT arsenic (+3 oxidation state) methyltransferase".

Further reading