2-Ketoarginine methyltransferase
| 2-Ketoarginine methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.243 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-Ketoarginine methyltransferase (EC 2.1.1.243, mrsA (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase.[1] This enzyme catalyses the following chemical reaction
This is a methylation reaction in which the methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from Pseudomonas syringae. It is involved in production of the rare amino acid 3-methylarginine.[2] Other organisms use it to incorporate that amino acid into arginomycin.[3]
References
- ↑ Enzyme 2.1.1.243 at KEGG Pathway Database.
- ↑ Braun SD, Hofmann J, Wensing A, Ullrich MS, Weingart H, Völksch B, et al. (April 2010). "Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93". Applied and Environmental Microbiology. 76 (8): 2500–2508. doi:10.1128/aem.00666-09. PMC 2849186. PMID 20190091.
- ↑ Feng J, Wu J, Gao J, Xia Z, Deng Z, He X (August 2014). "Biosynthesis of the β-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941". Applied and Environmental Microbiology. 80 (16): 5021–5027. doi:10.1128/AEM.01172-14. PMC 4135772. PMID 24907335.
External links
- 2-ketoarginine+methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Category:

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