Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.137 - arsenite methyltransferase and Organism(s) Mus musculus and UniProt Accession Q91WU5

for references in articles please use BRENDA:EC2.1.1.137
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.137 arsenite methyltransferase
IUBMB Comments
An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes or detoxification of inorganic arsenous acid in animals. The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism) , from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues via a disulfide bond cascade pathway [7, 8]. Most of the substrates undergo two methylations and are converted to dimethylarsinous acid . However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane. Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system. The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q91WU5
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
as3mt, arsenic (+3 oxidation state) methyltransferase, n6amt1, has3mt, arsenite methyltransferase, cyt19, as(iii) s-adenosylmethionine methyltransferase, arsenic (iii) methyltransferase, arsenite s-adenosylmethionine methyltransferase, arsenic (+3) methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
arsenite (+3 oxidation state) methyltransferase
-
arsenic (+3 oxidation state) methyltransferase
-
-
ArsM
-
-
-
-
ArsM protein
-
-
AS3MT
methylarsonite methyltransferase
-
-
-
-
S-adenosyl-L-methionine:arsenic(III) methyltransferase
-
-
-
-
S-adenosyl-L-methionine:methylarsonite As-methyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
reaction mechanism, overview
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
reaction modelling, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transfer of methyl group
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:arsenous acid As-methyltransferase
An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes [11] or detoxification of inorganic arsenous acid in animals. The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism) [6], from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues [10] via a disulfide bond cascade pathway [7, 8]. Most of the substrates undergo two methylations and are converted to dimethylarsinous acid [9]. However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane. Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system. The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
CAS REGISTRY NUMBER
COMMENTARY hide
167140-41-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
additional information
?
-
-
enzyme evolutionary analysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
show the reaction diagram
-
-
-
?
additional information
?
-
-
enzyme evolutionary analysis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000000367
-
lung
0.00000000667
-
liver
0.0000000117
-
kidney
0.0000000241
-
testis
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AS3MT_MOUSE
376
0
41794
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Healey, S.M.; Casarez, E.A.; Ayalo-Fierro, F.; Aposhian, H.V.
Enzymatic methylation of arsenic compoundes. Arsenite methyltransferase activity in tissues of mice
Toxicol. Appl. Pharmacol.
148
65-70
1998
Mus musculus
Manually annotated by BRENDA team
Thomas, D.J.; Li, J.; Waters, S.B.; Xing, W.; Adair, B.M.; Drobna, Z.; Devesa, V.; Styblo, M.
Arsenic (+3 oxidation state) methyltransferase and the methylation of arsenicals
Exp. Biol. Med.
232
3-13
2007
Bos taurus, Bos taurus (Q58DQ0), Ciona intestinalis, Gallus gallus, Homo sapiens (Q9HBK9), Mus musculus, no activity in Caenorhabditis elegans, no activity in Drosophila melanogaster, Oncorhynchus mykiss, Pan troglodytes, Rattus norvegicus, Rattus norvegicus (Q8VHT6), Rhodopseudomonas palustris, Strongylocentrotus purpuratus
Manually annotated by BRENDA team
John, J.P.; Oh, J.E.; Pollak, A.; Lubec, G.
Identification and characterisation of arsenite (+3 oxidation state) methyltransferase (AS3MT) in mouse neuroblastoma cell line N1E-115
Amino Acids
35
355-358
2008
Mus musculus (Q91WU5), Mus musculus
Manually annotated by BRENDA team