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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

Engineering

Engineering on EC 2.1.1.137 - arsenite methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C186S
-
mutation abolishes the capability of As(III) methylation
C238S
-
mutation abolishes the capability of As(III) methylation
C59S
-
mutation abolishes the capability of As(III) methylation
C10S
activtiy similar to wild-type
C10S/C11S/C193S/C268S
mutant dispays activity
C11S
activity similar to wild-type
C145S
loss of catalytic activity
C193S
activity similar to wild-type
C195S
loss of catalytic activity
C268S
activity similar to wild-type
C174A
Cyanidioschyzon sp.
-
the mutation leads to loss of As(III) methylation
C224A
Cyanidioschyzon sp.
-
the mutation leads to loss of As(III) methylation
C72A
Cyanidioschyzon sp.
-
the mutation leads to loss of As(III) methylation, but still shows trivalent methylarsenate methylation
Y70W
Cyanidioschyzon sp.
-
the mutant exhibits metalloid binding
C44A
mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate
C44A/C72A
mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate
C165S
-
inactive
C210S
-
inactive
C250S
the mutation favors S-adenosyl-L-methionine binding to the enzyme
C271S
-
the mutation does not affect the activity and structure of the enzyme
C334S
-
the mutation decreases the enzymatic turnover and changes the conformation of the enzyme
C360S
-
the mutation decreases the enzymatic turnover and changes the conformation of the enzyme
C375S
-
the mutation does not affect the activity and structure of the enzyme
C72S
-
the mutant is completely inactive
D102N
inactive
D102P
inactive
D150N
the mutant shows reduced activity compared to the wild type enzyme
D150P
inactive
D76N
inactive
D76P
inactive
D84N
inactive
D84P
inactive
G134A
the mutant’s activity is seriously impaired compared with that of wild type
G60A
inactive
G80A
inactive
G82A
the mutant’s activity is seriously impaired compared with that of wild type
I101A
inactive
L160A
inactive
L77A
the mutant’s activity is seriously impaired compared with that of wild type
M287T
N155A
inactive
R57A
the mutant's activity is seriously impaired compared with that of wild type
R83A
the mutant’s activity is seriously impaired compared with that of wild type
S81A
the mutant’s activity is seriously impaired compared with that of wild type
T104A
the mutant’s activity is seriously impaired compared with that of wild type
V157A
the mutant’s activity is seriously impaired compared with that of wild type
V161A
the mutant’s activity is seriously impaired compared with that of wild type
Y135A
the mutant’s activity is seriously impaired compared with that of wild type
Y58A
the mutant’s activity is seriously impaired compared with that of wild type
additional information
-
an exon-4 and -5 skipping (DELTA4,5) truncated mutant form does not convert arsenite to monomethylarsonate or dimethylarsinic acid