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A single amino acid determines position specificity of an Arabidopsis thaliana CCoAOMT‐like O ‐methyltransferase
Author(s) -
Wils Christopher Ralf,
Brandt Wolfgang,
Manke Kerstin,
Vogt Thomas
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.01.040
Subject(s) - o methyltransferase , arabidopsis thaliana , biochemistry , methylation , chemistry , methyltransferase , enzyme , amino acid , arabidopsis , biology , gene , mutant
Caffeoyl‐coenzyme A O ‐methyltransferase (CCoAOMT)‐like proteins from plants display a conserved position specificity towards the meta ‐position of aromatic vicinal dihydroxy groups, consistent with the methylation pattern observed in vivo. A CCoAOMT‐like enzyme identified from Arabidopsis thaliana encoded by the gene At4g26220 shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta‐ position. Sequence alignments and homology modelling identified several unique amino acids compared to motifs of other CCoAOMT‐like enzymes. Mutation of a single glycine, G46 towards a tyrosine was sufficient for a reversal of the unusual para ‐ back to meta ‐ O ‐methylation of flavanones and dihydroflavonols.