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B6db references: d9dd

type Journal Article
authors Tossaton Charoonratana, Juraithip Wungsintaweekul , Niwat Keawpradub and Rob Verpoorte2
title Molecular cloning and expression of tryptophan decarboxylase from Mitragyna speciosa
journal Acta Physiologiae Plantarum
Activity 4.1.1.28
Family 4.1.1.28
sel selected
year (2013)
volume 35
number 8
pages 2611-2621
 
abstract Tryptophan decarboxylase (TDC) catalyzes the decarboxylation of tryptophan to tryptamine in mitragynine biosynthesis via the shikimate pathway. Using the rapid amplification of cDNA ends (RACE) technique, the gene encoding TDC from Mitragyna speciosa was cloned (designated as MsTDC). The MsTDC cDNA contained an open reading frame (ORF) of 1,521 base pairs (bp) encoding 506 amino acid residues. It had a pyridoxal-phosphate (PLP)-binding site at the amino acid position 313334 residues. The MsTDC showed homology of 6876 % to the TDC of other plants. Heterologous expression in Escherichia coli afforded the soluble proteins as an apparent band of 57 kDa as judged by SDS-PAGE. Expression of the MsTDC in M. speciosa hairy roots under the 35S promoter was performed by insertion of MsTDC into pCAMBIA1300-gfp. The transgenic hairy root lines were detected by fluorescence microscopy and showed an increased accumulation of tryptamine.
last changed 2014/03/06 12:09

B6db references