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   <subfield code="a">Evolution of Novel O -methyltransferases from the Vanilla planifolia Caffeic Acid O -methyltransferase</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Huaijun Li, David Rotter, Thomas Hartman, Fulya Pak, Daphna Havkin-Frenkel, Faith Belanger]</subfield>
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   <subfield code="a">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.</subfield>
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   <subfield code="a">O -methyltransferase</subfield>
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   <subfield code="a">secondary metabolites</subfield>
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   <subfield code="a">IEMT : (iso)eugenol O-methyltransferase</subfield>
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   <subfield code="a">PCR : polymerase chain reaction</subfield>
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   <subfield code="a">SAM : S-adenosyl-l-methionine</subfield>
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