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. 2016 May 27;14(9):1108–1123. doi: 10.1080/15476286.2016.1191737

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© 2017 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 4. — Different views of DNMT2 in surface representation. The residues subjected to mutagenesis are colored according to their residual activity. The cofactor product S-adenosyl-l-homocysteine is colored blue. Panel A shows that residues which strongly interfere with catalysis (colored red here) cluster on the “front” face of the enzyme and surround a cleft that also contains the SAM binding pocket and the catalytic residues. Panel B represents a view of the “back side” of the enzyme after a 180° rotation of the view shown in panel A about the vertical axis. Reproduced from⁴⁸ with permission. Copyright (2012) American Chemical Society.