Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity.

Planta
Bong-Gyu KimJoong-Hoon Ahn

Abstract

O-Methyltransferase (OMT) catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to hydroxyl groups of methyl acceptors. Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2 with several phenolic compounds, including quercetin and caffeoyl-CoA. To determine the critical amino acids for the different reactivity of the two OMTs, site-directed mutagenesis was carried out. The amino acid proline at position 35 in PaOMT2 and leucine in PaOMT3 is a critical amino acid for their reactivity. Molecular modeling showed that the sequential change triggered by Leu35 resulted in a change in the size of the substrate binding pocket, which could account for the different catalytic reactivity of two OMTs.

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Citations

Feb 12, 2014·Journal of Agricultural and Food Chemistry·Shama V JosephBritt M Burton-Freeman
Mar 2, 2017·The New Phytologist·Tanja PaaselaTeemu H Teeri
Jul 4, 2018·International Journal of Molecular Sciences·Bin SunSheng Xu

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