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. Author manuscript; available in PMC: 2012 May 25.
Published in final edited form as: J Am Chem Soc. 2011 May 3;133(20):7648–7651. doi: 10.1021/ja2006719

Figure 2.

Figure 2

(a) Enzymatic activity of PRMT1 and its mutants on RGG peptide substrate with SAM analogues as cofactors (SAM, 1 and SAM analogues 2–5). Letters “m” and “d” refer to mono- and di-modifications. Color boxes code for percentages of modification under our assay conditions; “ND” means nondetectable with the current MS assay. (b) Representative LC-ESI mass spectra of RGG peptide 4-propargyloxy-but-2-enylated by M48G and Y39FM48G PRMT1 mutants, respectively. Given that the alkylation does not affect the ionization efficiency of the RGG peptide (Figure S1B), the co-eluted LC-MS peaks of the unmodified and modified peptides were co-integrated to obtain the mass ratios and calculated the percentage of conversion (see supporting information for details).