Benzaldehyde dehydrogenase from chitosan-treated Sorbus aucuparia cell cultures

Gaid, Mariam; Sircar, Debabrata; Beuerle, Till; Mitra, Adinpunya; Beerhues, Ludger

doi:10.1016/j.jplph.2009.03.003

Cited by 22 publications

(22 citation statements)

References 16 publications

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“…Which biosynthetic route is used in S. aucuparia cell cultures is still open. Recently, benzaldehyde dehydrogenase was detected in elicitor-treated S. aucuparia cell cultures, suggesting that a benzoic acid biosynthetic route via benzaldehyde is operative (Gaid et al 2009). Benzaldehyde dehydrogenase exhibited only low relative activity with salicylaldehyde, likewise pointing to a minor role of the 2-hydroxylated intermediates in benzoic acid metabolism of elicitor-treated S. aucuparia cell cultures.…”

Section: Discussionmentioning

confidence: 99%

A novel 4-hydroxycoumarin biosynthetic pathway

et al. 2009

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Coumarin forms in melilotoside (trans-ortho-coumaric acid glucoside)-containing plant species upon cell damage. In moldy melilotoside-containing plant material, trans-ortho-coumaric acid is converted by fungi to 4-hydroxycoumarin, two molecules of which spontaneously combine with formaldehyde to give dicoumarol. Dicoumarol causes internal bleeding in livestock and is the forerunner of the warfarin group of medicinal anticoagulants. Here, we report 4-hydroxycoumarin formation by biphenyl synthase (BIS). Two new BIS cDNAs were isolated from elicitor-treated Sorbus aucuparia cell cultures. The encoded isoenzymes preferred ortho-hydroxybenzoyl (salicoyl)-CoA as a starter substrate and catalyzed a single decarboxylative condensation with malonyl-CoA to give 4-hydroxycoumarin. When elicitor-treated S. aucuparia cell cultures were fed with the N-acetylcysteamine thioester of salicylic acid, 4-hydroxycoumarin accumulated in the culture medium. Incubation of the BIS isoenzymes with benzoyl-CoA and malonyl-CoA resulted in the formation of 3,5-dihydroxybiphenyl which is the precursor of the phytoalexins of the Maloideae.

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Section: Discussionmentioning

confidence: 99%

A novel 4-hydroxycoumarin biosynthetic pathway

et al. 2009

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“…The reaction was stopped by adding ice-cold acetic acid: methanol (1:9, v/v) in 1:1 ratio followed by centrifugation at 10,0009g for 10 min, and the resultant supernatant was analyzed by HPLC. The chemical identity of the enzymatic product was confirmed by co-chromatography with authentic standard, UV-spectroscopy and finally by GC-MS analysis (Gaid et al 2009). …”

Section: P-hydroxybenzaldehyde Dehydrogenase Assaymentioning

confidence: 99%

Characterization of p-hydroxybenzaldehyde dehydrogenase, the final enzyme of p-hydroxybenzoic acid biosynthesis in hairy roots of Daucus carota

et al. 2011

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Hairy root cultures of Daucus carota respond to methyl-jasmonate treatment with enhanced accumulation of p-hydroxybenzoic acid. The final C 1 -side chain of this compound is shaped by p-hydroxybenzaldehyde dehydrogenase (HBD) that catalyzes the formation of p-hydroxybenzoic acid from p-hydroxybenzaldehyde in the presence of NAD ? . HBD was biochemically characterized from cell-free hairy root extracts of D. carota. The preferred substrate for HBD was p-hydroxybenzaldehyde. The apparent K m values were 54.8 and 74.4 lM for p-hydroxybenzaldehyde and NAD ? , respectively. Divalent metal cations did not significantly affect enzyme activity.

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“…A cDNA encoding benzaldehyde dehydrogenase has recently been cloned from A. majus, the flowers of which emit high levels of methylbenzoate (Long et al, 2009). The enzyme has also been detected in cell cultures of Sorbus aucuparia, and its properties have been studied (Gaid et al, 2009). Furthermore, a gene encoding aldehyde oxidase, which was purified from Arabidopsis and exhibited high affinity for benzaldehyde, was identified ).…”

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Cinnamate:CoA Ligase Initiates the Biosynthesis of a Benzoate-Derived Xanthone Phytoalexin in Hypericum calycinum Cell Cultures

Gaid

Sircar²,

Müller³

et al. 2012

Plant Physiology

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Although a number of plant natural products are derived from benzoic acid, the biosynthesis of this structurally simple precursor is poorly understood. Hypericum calycinum cell cultures accumulate a benzoic acid-derived xanthone phytoalexin, hyperxanthone E, in response to elicitor treatment. Using a subtracted complementary DNA (cDNA) library and sequence information about conserved coenzyme A (CoA) ligase motifs, a cDNA encoding cinnamate:CoA ligase (CNL) was isolated. This enzyme channels metabolic flux from the general phenylpropanoid pathway into benzenoid metabolism. HcCNL preferred cinnamic acid as a substrate but failed to activate benzoic acid. Enzyme activity was strictly dependent on the presence of Mg2+ and K+ at optimum concentrations of 2.5 and 100 mm, respectively. Coordinated increases in the Phe ammonia-lyase and HcCNL transcript levels preceded the accumulation of hyperxanthone E in cell cultures of H. calycinum after the addition of the elicitor. HcCNL contained a carboxyl-terminal type 1 peroxisomal targeting signal made up by the tripeptide Ser-Arg-Leu, which directed an amino-terminal reporter fusion to the peroxisomes. Masking the targeting signal by carboxyl-terminal reporter fusion led to cytoplasmic localization. A phylogenetic tree consisted of two evolutionarily distinct clusters. One cluster was formed by CoA ligases related to benzenoid metabolism, including HcCNL. The other cluster comprised 4-coumarate:CoA ligases from spermatophytes, ferns, and mosses, indicating divergence of the two clades prior to the divergence of the higher plant lineages.

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Benzaldehyde dehydrogenase from chitosan-treated Sorbus aucuparia cell cultures

Cited by 22 publications

References 16 publications

A novel 4-hydroxycoumarin biosynthetic pathway

A novel 4-hydroxycoumarin biosynthetic pathway

Characterization of p-hydroxybenzaldehyde dehydrogenase, the final enzyme of p-hydroxybenzoic acid biosynthesis in hairy roots of Daucus carota

Cinnamate:CoA Ligase Initiates the Biosynthesis of a Benzoate-Derived Xanthone Phytoalexin in Hypericum calycinum Cell Cultures

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