ID: | 2.1.1.137 |
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Description: | Arsenite methyltransferase. |
Alternative Name: |
S-adenosyl-L-methionine:methylarsonite As-methyltransferase. S-adenosyl-L-methionine:arsenic(III) methyltransferase. Methylarsonite methyltransferase. |
Cath: | 1.20.1050.10; 3.40.250.10; 3.40.30.10; 3.40.50.2300; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.1.1.137 |
BRENDA Enzyme Link: | BRENDA 2.1.1.137 |
KEGG Enzyme Link: | KEGG2.1.1.137 |
BioCyc Enzyme Link: | BioCyc 2.1.1.137 |
ExPASy Enzyme Link: | ExPASy2.1.1.137 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.137 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.137 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.137 |
IntEnz Enzyme Link: | IntEnz 2.1.1.137 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.137 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:15293 | arsenite + S-adenosyl-L-methionine = H(+) + methylarsonate + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[As;H0;+0:2](-[*:3])-[OH;+0:4].[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:8]>>[*:1]-[As;H0;+0:2](-[*:3])(-[CH3;+0:8])=[O;H0;+0:4].[*:5]-[S;H0;+0:6]-[*:7] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver. | Zakharyan R, Wu Y, Bogdan GM, Aposhian HV | 1995 Dec | 8605285 |
A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol. | Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL, Simeonsson JB, Thomas DJ | 2002 Mar 29 | 11790780 |
Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. | Zakharyan RA, Aposhian HV | 1999 Dec | 10604879 |
Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes. | Zakharyan RA, Ayala-Fierro F, Cullen WR, Carter DM, Aposhian HV | 1999 Jul 1 | 10387927 |
RHEA:11684 | methylarsonous acid + S-adenosyl-L-methionine = dimethylarsinate + 2 H(+) + S-adenosyl-L-homocysteine |
RULE(radius=1) | [*:1]-[As;H0;+0:2](-[*:3])-[OH;+0:4].[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:8]>>[*:1]-[As;H0;+0:2](-[*:3])(-[CH3;+0:8])=[O;H0;+0:4].[*:5]-[S;H0;+0:6]-[*:7] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver. | Zakharyan R, Wu Y, Bogdan GM, Aposhian HV | 1995 Dec | 8605285 |
A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol. | Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL, Simeonsson JB, Thomas DJ | 2002 Mar 29 | 11790780 |
Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. | Zakharyan RA, Aposhian HV | 1999 Dec | 10604879 |
Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes. | Zakharyan RA, Ayala-Fierro F, Cullen WR, Carter DM, Aposhian HV | 1999 Jul 1 | 10387927 |
Interactive Effects of N6AMT1 and As3MT in Arsenic Biomethylation. | Zhang H, Ge Y, He P, Chen X, Carina A, Qiu Y, Aga DS, Ren X | 2015 Aug | 25997655 |
Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) in arsenic biomethylation and its role in arsenic-induced toxicity. | Ren X, Aleshin M, Jo WJ, Dills R, Kalman DA, Vulpe CD, Smith MT, Zhang L | 2011 Jun | 21193388 |