Characterization of a multifunctional methyltransferase from the orchid Vanilla planifolia
| Autor: | S. Gropper, Faith C. Belanger, D. Havkin-Frenkel, W. D. Dai, F. E. Pak |
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| Rok vydání: | 2003 |
| Předmět: |
Methyltransferase
DNA Complementary Molecular Sequence Data Plant Science Polymerase Chain Reaction Substrate Specificity chemistry.chemical_compound Complementary DNA Amino Acid Sequence Cloning Molecular Vanilla Flavor Cells Cultured Conserved Sequence Phylogeny Triticum DNA Primers chemistry.chemical_classification biology Base Sequence Sequence Homology Amino Acid Vanillin Substrate (chemistry) General Medicine Methylation Methyltransferases biology.organism_classification Peptide Fragments Recombinant Proteins Vanilla planifolia Enzyme chemistry Biochemistry Agronomy and Crop Science Sequence Alignment Medicago sativa |
| Zdroj: | Plant cell reports. 22(12) |
| ISSN: | 0721-7714 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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