| EC |
2.1.1.301 |
| Accepted name: |
cypemycin N-terminal methyltransferase |
| Reaction: |
2 S-adenosyl-L-methionine + N-terminal L-alanine-[cypemycin] = 2 S-adenosyl-L-homocysteine + N-terminal N,N-dimethyl-L-alanine-[cypemycin] |
| Other name(s): |
CypM |
| Systematic name: |
S-adenosyl-L-methionine:N-terminal L-alanine-[cypemycin] N-methyltransferase |
| Comments: |
The enzyme, isolated from the bacterium Streptomyces sp. OH-4156, can methylate a variety of linear oligopeptides, cyclic peptides such as nisin and haloduracin, and the ε-amino group of lysine [2]. Cypemycin is a peptide antibiotic, a member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Claesen, J. and Bibb, M. Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides. Proc. Natl. Acad. Sci. USA 107 (2010) 16297–16302. [DOI] [PMID: 20805503] |
| 2. |
Zhang, Q. and van der Donk, W.A. Catalytic promiscuity of a bacterial α-N-methyltransferase. FEBS Lett. 586 (2012) 3391–3397. [DOI] [PMID: 22841713] |
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| [EC 2.1.1.301 created 2014] |
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