| EC |
2.1.1.381 |
| Accepted name: |
arginine Nω-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + L-arginine = S-adenosyl-L-homocysteine + Nω-methyl-L-arginine |
| Other name(s): |
sznE (gene name); stzE (gene name) |
| Systematic name: |
S-adenosyl-L-methionine:L-arginine Nω-methyltransferase |
| Comments: |
The enzyme, characterized from the bacterium Streptomyces achromogenes subsp. streptozoticus, participates in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Ng, T.L., Rohac, R., Mitchell, A.J., Boal, A.K. and Balskus, E.P. An N-nitrosating metalloenzyme constructs the pharmacophore of streptozotocin. Nature 566 (2019) 94–99. [DOI] [PMID: 30728519] |
| 2. |
He, H.Y., Henderson, A.C., Du, Y.L. and Ryan, K.S. Two-enzyme pathway links l-arginine to nitric oxide in N-nitroso biosynthesis. J. Am. Chem. Soc. 141 (2019) 4026–4033. [DOI] [PMID: 30763082] |
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| [EC 2.1.1.381 created 2021] |
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