Plant Cell Reports

, Volume 22, Issue 12, pp 959–966

Characterization of a multifunctional methyltransferase from the orchid Vanilla planifolia

  • F. E. Pak
  • S. Gropper
  • W. D. Dai
  • D. Havkin-Frenkel
  • F. C. Belanger
Physiology and Biochemistry

DOI: 10.1007/s00299-004-0795-x

Cite this article as:
Pak, F.E., Gropper, S., Dai, W.D. et al. Plant Cell Rep (2004) 22: 959. doi:10.1007/s00299-004-0795-x

Abstract

The final enzymatic step in the synthesis of the flavor compound vanillin (4-hydroxy-3-methoxybenzaldehyde) is believed to be methylation of 3,4-dihydroxybenzaldehyde. We have isolated and functionally characterized a cDNA that encodes a multifunctional methyltransferase from Vanilla planifolia tissue cultures that can catalyze the conversion of 3,4-dihydroxybenzaldehyde to vanillin, although 3,4-dihydroxybenzaldehyde is not the preferred substrate. The higher catalytic efficiency of the purified recombinant enzyme with the substrates caffeoyl aldehyde and 5-OH-coniferaldehyde, and its tissue distribution, suggest this methyltransferase may primarily function in lignin biosynthesis. However, since the enzyme characterized here does have 3,4-dihydroxybenzaldehyde-O-methyltransferase activity, it may be useful in engineering strategies for the synthesis of natural vanillin from alternate sources.

Keywords

Caffeic acid methyltransferase3,4-DihydroxybenzaldehydeVanillin

Abbreviations

COMT

Caffeic acid O-methyltransferase

DOMT

3,4-Dihydroxybenzaldehyde-O-methyltransferase

OMTs

O-Methyltransferases

SAM

S-adenosyl-l-methionine

Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  • F. E. Pak
    • 1
  • S. Gropper
    • 1
  • W. D. Dai
    • 1
  • D. Havkin-Frenkel
    • 1
  • F. C. Belanger
    • 1
  1. 1.Department of Plant Biology and PathologyRutgers UniversityNew BrunswickUSA