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. 2019 Aug 7;9(8):163. doi: 10.3390/metabo9080163

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Mutagenesis analysis of the oat CCoAOMT enzyme. (A) Sequence alignment of oat CCoAOMT sequence and related sequences. Conserved residues involved in SAM binding were highlighted in red boxes. Residues involved in divalent binding were highlighted in green boxes. The loop region was between N227 to L250. Mutation site were marked by red *. Changes in the activity of native and mutagenized CCoAOMT proteins on three substrates avenanthramide C (B), caffeoyl-CoA (C), and caffeic acid (D) were calculated using the average of three biological triplicate measurements.