A methyltransferase for synthesis of the phytoalexin 6‐methoxymellein in carrot cells

@article{Kurosaki1988AMF,
  title={A methyltransferase for synthesis of the phytoalexin 6‐methoxymellein in carrot cells},
  author={Fumiya Kurosaki and Arasuke Nishi},
  journal={FEBS Letters},
  year={1988},
  volume={227}
}
Carrot (Daucus carota L.) roots treated with 2‐chloroethylphosphonic acid or uronide elicitor accumulated the phytoalexin 6‐methoxymellein. The extracts of these cells catalyzed methylation of 6‐hydroxymellein to 6‐methoxymellein with S‐adenosyl‐L‐methionine as a methyl donor. Activity of the O‐methyltransferase was not found in fresh carrot roots but increased when they were treated with either type of elicitor in parallel with the increase in 6‐methoxymellein content. The enzyme did not… 
Induction of 6-methoxymellein 6-hydroxymellein production in carrot cells
TLDR
Changes in pH values at the moment of elicitation of carrot cell suspension cultures influenced the amounts of both phytoalexins synthesized.
Comparison of enzyme activities involved in the biosynthesis of carrot phytoalexin 6-methoxymellein
Abstract Enzyme activities involved in carrot phytoalexin 6-methoxymellein biosynthesis were determined by an improved assay method. Irrespective of the elicitor such as a metal ion, ethylene or
Elicitor induction of enzyme activities and 6-methoxymellein production in carrot cell suspension culture
TLDR
Fusarium moniliforme endo-polygalacturonase and an elicitor preparation derived from the cell walls of Phythophthora megasperma induced in carrot cell suspension cultures stimulated a marked increase of phenylalanine ammonia-lyase (PAL) activity without affecting chalcone synthase (CHS) activity.
6‐Hydroxymellein synthetase as a multifunctional enzyme complex in elicitor‐treated carrot root extract
TLDR
Observations suggest that the biosynthesis of 6‐hydroxymellein in carrot cells is catalyzed by an enzyme consisting of a single peptide chain.
Regulation of biosynthesis of carrot phytoalexin 6-methoxymellein
TLDR
The results suggest that 6MM synthetic enzymes have high affinities for acyl-CoAs and S -adenosyl- l -methionine and preferentially utilize these substrates as compared with other constitutive enzymes.
Derailment product in NADPH-dependent synthesis of a dihydroisocoumarin 6-hydroxymellein by elicitor-treated carrot cell extracts.
TLDR
This finding suggested that the reduction of the double bond at the 3,4-position of the phytoalexin takes place during the elongation of the poly(oxomethylene) chain.
Partial purification and characterization of 6-hydroxymellein-O-methyltransferase from elicitor-treated carrot cells
Abstract 6-Hydroxymellein-O-methyltransferase (6HMOMT), an inducible OMT involved in the biosynthesis of the carrot phytoalexin 6-methoxymellein (6MM), was partially purified with a 105-fold increase
Transacylase‐like structure and its role in substrate channeling of 6‐hydroxymellein synthase, a multifunctional polyketide biosynthetic enzyme in carrot cell extracts
TLDR
It is suggested that transacylase‐like domain is involved in the structure of 6‐hydroxymellein synthase as a common primary binding site of its co‐substrates, and acetyl and malonyl moieties are properly channeled from their CoA esters to cysteine‐SH and acyl carrier protein‐SH via this domain, respectively.
Biosynthesis of phytoalexin in carrot root requires ethylene action.
TLDR
The role of ethylene in phytoalexin production by carrot roots was investigated using the ethylene action inhibitor 1-methylcyclopropene (MCP), indicating that 6-ME synthesis by carrot Roots requires ethyleneaction.
Phytoalexin production and cell death in elicited carrot cell suspension cultures
TLDR
Production of the carrot phytoalexin and its immediate biosynthetic precursor, 6-hydroxymellein, was induced in suspension cultures by biotic elicitors and by the abiotic elicitor HgCl2.
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