| Arsenite methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.137 | ||||||||
| CAS no. | 167140-41-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Arsenite methyltransferase ( EC 2.1.1.137, S-adenosyl-L-methionine:arsenic(III) methyltransferase, S-adenosyl-L-methionine:methylarsonite As-methyltransferase, methylarsonite methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:arsenite As-methyltransferase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
- (1) S-adenosyl-L-methionine + arsenite S-adenosyl-L-homocysteine + methylarsonate
- (2) S-adenosyl-L-methionine + methylarsonite S-adenosyl-L-homocysteine + dimethylarsinate
An enzyme of the biotransformation pathway that forms dimethylarsinate from inorganic arsenite and arsenate.
- ^ Zakharyan RA, Aposhian HV (December 1999). "Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase". Chemical Research in Toxicology. 12 (12): 1278–83. doi: 10.1021/tx9901231. PMID 10604879.
- ^ Zakharyan RA, Ayala-Fierro F, Cullen WR, Carter DM, Aposhian HV (July 1999). "Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes". Toxicology and Applied Pharmacology. 158 (1): 9–15. doi: 10.1006/taap.1999.8687. PMID 10387927.
- ^ Zakharyan RA, Wildfang E, Aposhian HV (September 1996). "Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic". Toxicology and Applied Pharmacology. 140 (1): 77–84. doi: 10.1006/taap.1996.0199. PMID 8806872.
- ^ Zakharyan R, Wu Y, Bogdan GM, Aposhian HV (December 1995). "Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver". Chemical Research in Toxicology. 8 (8): 1029–38. doi: 10.1021/tx00050a006. PMID 8605285.
- ^ Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL, Simeonsson JB, Thomas DJ (March 2002). "A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol". The Journal of Biological Chemistry. 277 (13): 10795–803. doi: 10.1074/jbc.M110246200. PMID 11790780.
- Arsenite+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Arsenite methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.137 | ||||||||
| CAS no. | 167140-41-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Arsenite methyltransferase ( EC 2.1.1.137, S-adenosyl-L-methionine:arsenic(III) methyltransferase, S-adenosyl-L-methionine:methylarsonite As-methyltransferase, methylarsonite methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:arsenite As-methyltransferase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
- (1) S-adenosyl-L-methionine + arsenite S-adenosyl-L-homocysteine + methylarsonate
- (2) S-adenosyl-L-methionine + methylarsonite S-adenosyl-L-homocysteine + dimethylarsinate
An enzyme of the biotransformation pathway that forms dimethylarsinate from inorganic arsenite and arsenate.
- ^ Zakharyan RA, Aposhian HV (December 1999). "Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase". Chemical Research in Toxicology. 12 (12): 1278–83. doi: 10.1021/tx9901231. PMID 10604879.
- ^ Zakharyan RA, Ayala-Fierro F, Cullen WR, Carter DM, Aposhian HV (July 1999). "Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes". Toxicology and Applied Pharmacology. 158 (1): 9–15. doi: 10.1006/taap.1999.8687. PMID 10387927.
- ^ Zakharyan RA, Wildfang E, Aposhian HV (September 1996). "Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic". Toxicology and Applied Pharmacology. 140 (1): 77–84. doi: 10.1006/taap.1996.0199. PMID 8806872.
- ^ Zakharyan R, Wu Y, Bogdan GM, Aposhian HV (December 1995). "Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver". Chemical Research in Toxicology. 8 (8): 1029–38. doi: 10.1021/tx00050a006. PMID 8605285.
- ^ Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL, Simeonsson JB, Thomas DJ (March 2002). "A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol". The Journal of Biological Chemistry. 277 (13): 10795–803. doi: 10.1074/jbc.M110246200. PMID 11790780.
- Arsenite+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)