Catalytic promiscuity of a bacterial Î±-N-methyltransferase

Article ID	Journal	Published Year	Pages	File Type
10871468	FEBS Letters	2012	7 Pages	PDF

Abstract

âº CypM can methylate both Î±-N-terminal amino groups and lysine Îµ-amino groups. âº CypM methylates a variety of cyclic peptides such as nisin and haloduracin. âº Î±-N-methyltransferases did not evolve as a specific clade.

Keywords

DMF MCMC Dehydrobutyrine N-methyl morpholine NMM SPPS Dehydroalanine S-adenosylhomocysteine SAH DHB SAM Peptide antibiotic Abu S-adenosylmethionine 2-aminobutyric acid DHA dimethylformamide Markov chain Monte Carlo Solid phase peptide synthesis Evolution Lantibiotic matrix assisted laser desorption ionization MALDI Catalytic promiscuity