Activating Compound | Comment | Organism | Structure |
---|---|---|---|
glutathione | ArsM is able to methylate As(III) in the presence of Cys without glutathione. In contrast, ArsM is not able to methylate As(III) in the presence of tris(2-carboxyethyl)phosphine without GSH | Bacillus sp. CX-1 |
Crystallization (Comment) | Organism |
---|---|
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 | Bacillus sp. CX-1 |
Protein Variants | Comment | Organism |
---|---|---|
C10S | activtiy similar to wild-type | Bacillus sp. CX-1 |
C10S/C11S/C193S/C268S | mutant dispays activity | Bacillus sp. CX-1 |
C11S | activity similar to wild-type | Bacillus sp. CX-1 |
C145S | loss of catalytic activity | Bacillus sp. CX-1 |
C193S | activity similar to wild-type | Bacillus sp. CX-1 |
C195S | loss of catalytic activity | Bacillus sp. CX-1 |
C268S | activity similar to wild-type | Bacillus sp. CX-1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus sp. CX-1 | A0A2P1M875 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + arsenite | - |
Bacillus sp. CX-1 | S-adenosyl-L-homocysteine + methylarsonate | - |
? | |
S-adenosyl-L-methionine + methylarsonite | - |
Bacillus sp. CX-1 | S-adenosyl-L-homocysteine + dimethylarsinate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 32000, calculated from sequence and SDS-PAGE, recombinant protein | Bacillus sp. CX-1 |
Organism | Comment | Expression |
---|---|---|
Bacillus sp. CX-1 | enzyme is constitutively expressed | additional information |
General Information | Comment | Organism |
---|---|---|
physiological function | expression of ArsM confers resistance to an As(III)-hypersensitive strain of Escherichia coli | Bacillus sp. CX-1 |