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2.1.1.137: arsenite methyltransferase

This is an abbreviated version!
For detailed information about arsenite methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.137

Reaction

2 S-adenosyl-L-methionine +

arsenic triglutathione
+ 2 thioredoxin +
H2O
=
S-adenosyl-L-homocysteine
+
dimethylarsinous acid
+ 3 glutathione + 2 thioredoxin disulfide

Synonyms

AdoMet:arsenic(III) methyltransferase, arsenic (+3 oxidation state) methyltransferase, arsenic (+3 oxidation state)-methyltransferase, arsenic (+3) methyltransferase, arsenic (III) methyltransferase, arsenic (III) S-adenosylmethionine methyltransferase, arsenic methyltransferase Cyt19, arsenic(III) methyltransferase, arsenite (+3 oxidation state) methyltransferase, arsenite methyltransferase, arsenite S-adenosylmethionine methyltransferase, ArsM, ArsM protein, ArsM7B, As(III) methyltransferase, As(III) S-adenosylmethionine methyltransferase, As(III) SAM methyltransferase, AS3MT, AsIII S-adenosylmethionine methyltransferase, Cyr19, Cyt19, EC 2.1.1.138, hAS3MT, methylarsonite methyltransferase, N6AMT1, S-adenosyl-L-methionine:arsenic(III) methyltransferase, S-adenosyl-L-methionine:methylarsonite As-methyltransferase, S-adenosylmethionine dependent arsenic methyltransferase, [As(III)] methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.137 arsenite methyltransferase

Crystallization

Crystallization on EC 2.1.1.137 - arsenite methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The two conserved cysteine residues Cys145 and Cys195 are in close propinquity and form an As(III) binding site. GSH forms the third ligand with As with the sulfur atom of GSH orienting toward the bound As(III) at approximately 2.4 A distance
hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3000, 0.1 M Tris-HCl, pH 7.0, containing 0.2 M calcium acetate
Cyanidioschyzon sp.
structure with the bound aromatic arsenicals phenylarsenite at 1.80 A resolution and reduced roxarsone at 2.25 A resolution. Compounds are bound to conserved residues C174 and C224. A loop containing Cys44 and Cys72 shifts by nearly 6.5 A in the arsenic(III)-bound structures compared with the SAM-bound structure