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. 2010 Aug 16;285(43):33037–33044. doi: 10.1074/jbc.M110.155283

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Biochemical characterization of hMTr1. A, activity of hMTr1 is dependent on SAM concentration. Reactions were performed with increasing SAM concentrations. Signals corresponding to cap0 and cap1 were quantified and expressed as a percentage of cap1 formed. B, activity of hMTr1 is inhibited by S-adenosylhomocysteine (SAH). Methylation reactions were performed in the presence of 5 μm SAM and increasing concentrations of S-adenosylhomocysteine. C, pH affects hMTr1 activity. Reactions were performed at the indicated pH in either Tris (filled circles) or bis-Tris (open circles). D, magnesium affects hMTr1 methyltransferase activity.