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Published on: April 1, 2016
Evolution of novel O-methyltransferases from the Vanilla planifolia caffeic acid O-methyltransferase
Huaijun Michael Li1, David Rotter, Thomas G Hartman
1Department of Plant Biology and Pathology and The Biotechnology Center for Agriculture & the Environment, Cook College, Rutgers University, 59 Dudley Road, New Brunswick, NJ 08901, USA.
Abstract:
The biosynthesis of many plant secondary compounds involves the methylation of one or more hydroxyl groups, catalyzed by O-methyltransferases (OMTs). Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the methylation of a single outer hydroxyl group in substrates possessing a 1,2,3-trihydroxybenzene moiety, such as methyl gallate and myricetin. This is a substrate requirement not previously reported for any OMTs. Based on sequence analysis these enzymes are most similar to caffeic acid O-methyltransferases (COMTs), but they have negligible activity with typical COMT substrates. Seven of 12 conserved substrate-binding residues in COMTs are altered in Van OMT-2 and Van OMT-3. Phylogenetic analysis of the sequences suggests that Van OMT-2 and Van OMT-3 evolved from the V. planifolia COMT. These V. planifolia OMTs are new instances of COMT-like enzymes with novel substrate preferences.
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