Enzymic Controls in the Biosynthesis of Lignin and Flavonoids

Hahlbrock, Klaus; Grisebach, Hans

doi:10.1146/annurev.pp.30.060179.000541

Cited by 390 publications

(202 citation statements)

References 28 publications

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“…3). The calculated molecular mass of the inferred amino-acid sequence is 75840 Da which agrees with estimates for the enzyme from other plants made by SDSjPAGE [17,181. The deduccd (Fig.…”

Section: Structirre Of'the Cdna Und the Amino M I D Sequence Of' P A supporting

confidence: 78%

Structure and some characterization of the gene for phenylalanine ammonia‐lyase from rice plants

Minami

Ozeki

Matsuoka

et al. 1989

European Journal of Biochemistry

137

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A nearly full-length cDNA and a genomic clone were isolated that encoded the phenylalanine ammonia-lyase (PAL) of rice plants. and the complete nucleotide sequences were determined. The gene encodes a polypeptide of 701 amino acid residues. The deduced amino acid sequence is highly similar to that of PAL from Phaseolus vulgaris deduced from an incomplete cDNA fragment. The cloned gene spans 4412 bp and consists of two exons and one intron. The site of initiation of transcription was located -86 nucleotides (position 1) upstream from the translational initiation codon by the primer-extension method. Sequences analogous to TATA-box and GCbox were found in the 5'-upstream region from the transcriptional initiation site. Southern blot analysis showed that the PAL gene of rice plants exists as a small multi-gene family. Within this family, the genomic clone isolated in this study was shown to be responsive by light. This also indicated that this genomic sequence functions as a gene for phenylalanine ammonia-lyase in rice plants in vivo.Phenylalanine ammonia-lyase (PAL} catalyzes the first reaction in the general pathway of biosynthesis of polyphenolic compounds including lignin, cinnamate esters and flavonoids [11, and is one of the key enzymes in the metabolism of these compounds [l]. The activity of PAL increases dramatically in response to various stimuli, such as wounding [2, 31, infection [4, 51, growth regulators [2] and light [6]. It is caused by de novo synthesis of the enzyme due to the increase in the amount of translatable mRNA, suggesting that activation of the gene expression may be induced by these stimuli [7, 81. However, no reports have shown the whole genomic structure or complete amino acid sequence of PAL. Furthermore, our knowledge on the regulatory mechanisms of PAL activity is limited to dicotyledonous plants. As a first step to elucidate the molecular mechanisms for the regulation of expression of the gene for PAL, we isolated a nearly full-sized cDNA and relevant genomic DNA for PAL from rice plant and analyzed their primary structures. Using a probe specific to the isolated genomic clone for PAL, we demonstrated the accumulation of the transcripts from this gene during greening. This also showed that the isolated genomic DNA functions as a gene for PAL in vivo. Corre MATERIALS AND METHODS Plant materialsRice (Oryza sativa L. cv. Nipponbare) seeds were sterilized in a 2% (massivol.) solution of sodium hypochlorite, washed extensively in tap water, and allowed to germinate on sterile vermiculite in a green house at 25 "C. Twelve days after germination, primary leaves (about 5 cm in length) were harvested, immediately frozen in liquid nitrogen, and used for extraction of poly(A)-rich RNA and high-molecular-mass DNA. In some experiments, plants were allowed to germinate in the dark for seven days, then illuminated at 200 pmol . m ~ . s ~ for various periods of time with fluorescent lights. At each stage of greening, plants were harvested and used for the extraction of total cellular RNA. Prepar...

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“…3). The calculated molecular mass of the inferred amino-acid sequence is 75840 Da which agrees with estimates for the enzyme from other plants made by SDSjPAGE [17,181. The deduccd (Fig.…”

Section: Structirre Of'the Cdna Und the Amino M I D Sequence Of' P A supporting

confidence: 78%

Structure and some characterization of the gene for phenylalanine ammonia‐lyase from rice plants

Minami

Ozeki

Matsuoka

et al. 1989

European Journal of Biochemistry

137

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“…iB) is similar to the biosynthetic pathways of flavonoids in other plants (13,14). Additionally, we have characterized and partially purified the rhamnosyl-transferase, as will be reported separately.…”

Section: Chalcone Synthasementioning

confidence: 62%

“…Chalconesynthase catalyzes the condensation of p-coumaryl-CoA with three molecules of malonyl-CoA yielding naringenin-chalcone (20). The substrate specificity of a 'naringin-chalconecyclase' activity, from immature grapefruit fruit (25), suggested that the flavonoid pathways in Citrus, might be different from the more studied flavonoid pathways of other plants (13,14) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

“…Little information is available on the biosynthetic pathways to flavanone-glycosides in Citrus (16). Chalcone-synthase is a key enzyme in the flavonoid pathway in several plants (13), but has not previously been reported in Citrus tissues. Chalconesynthase catalyzes the condensation of p-coumaryl-CoA with three molecules of malonyl-CoA yielding naringenin-chalcone (20).…”

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confidence: 96%

“…They suggested that hydroxylation and methylation of naringenin to form hesperetin occurred after glycosylation as the chalcone isomerase did not isomerize neohesperidin chalcone (25). This is in contrast to other plants where hydroxylations and methylations occur before glycosylation (13,14 (13,14) have been found in Citrus tissues, including phenylalanine ammonia-lyase (23,26,30), cinnamate 4-hydroxylase (15) and chalcone isomerase (23,28). The chalcone isomerase from Citrus peels catalyzed the reversible conversion of chalcones to their isomeric flavanones (28).…”

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confidence: 99%

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Flavanone Glycoside Biosynthesis in Citrus

Lewinsohn

Britsch²,

Mazur³

et al. 1989

Plant Physiol.

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Previous indirect evidence suggested that the biosynthesis of flavonoids in Citrus may not proceed via the usual chalcone synthase reaction and that glycosylation occurs during chalcone formation and not afterward, as has been reported in other species. We detected chalcone-synthase and UDP-glucose:flavanone-7-O-glucosyl-transferase activities in cell-free extracts of Citrus. The glucosylated flavanone was further rhamnosylated when exogenous UDP-glucose and NADPH were added to the extract. Chalcone-synthase activity was detected in cellfree extracts derived from young leaves and fruits. Young fruits (2 millimeter diameter) had the highest chalcone synthase activity. UDP-glucose:flavanone-7-0-glucosyl-transferase activity was measured in cell-free extracts derived from young leaves and fruits of Citrus mitis and Citrus maxima. The highest UDP-glucose:flavanone-7-O-glucosyl-transferase activity was found in young C. maxima leaves. These data indicate that Citrus contains a flavonoid pathway similar to that studied in other species.Several Citrus spp. (Rutaceae) contain bitter tasting flavanone-disaccharides (18). They are used as food additives for their flavor or can be converted by hydrogenation into the extremely sweet dihydrochalcone derivatives (18). Little information is available on the biosynthetic pathways to flavanone-glycosides in Citrus (16). Chalcone-synthase is a key enzyme in the flavonoid pathway in several plants (13), but has not previously been reported in Citrus tissues. Chalconesynthase catalyzes the condensation of p-coumaryl-CoA with three molecules of malonyl-CoA yielding naringenin-chalcone (20). The substrate specificity of a 'naringin-chalconecyclase' activity, from immature grapefruit fruit (25), suggested that the flavonoid pathways in Citrus, might be different from the more studied flavonoid pathways of other plants (13,14) (Fig. 1). They interpreted their results (25) as suggesting that glucosylation and rhamnosylation occurred during chalcone formation in Citrus, as the aglycones were not ' Supported by a Minerva foundation travel grant. Present address:

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High Performance Liquid Chromatography and Photodiode Array Detection of Phenylpropanoids and Benzoates inRubus Protoplasts Elicited by Kinetin

Chevolot

Dubois-Dauphin

Yvin³

et al. 1997

Phytochem. Anal.

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Reverse‐phase high performance liquid chromatography with photodiode array detection (PAD) has been developed for simultaneous separation, identification and quantification of picomoles of phenylalanine ammonia‐lyase (PAL) reaction products. Separation has been achieved in 30 min on a reverse‐phase silica column using methanol:water gradient elution, and PAD provided sensitive and specific determination of phenolics. The method has been applied to biological samples to study kinetin‐induced changes in phenol pathways within protoplasts of Rubus fruticosus (raspberry). © 1997 by John Wiley & Sons, Ltd.

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Enzymic Controls in the Biosynthesis of Lignin and Flavonoids

Cited by 390 publications

References 28 publications

Structure and some characterization of the gene for phenylalanine ammonia‐lyase from rice plants

Structure and some characterization of the gene for phenylalanine ammonia‐lyase from rice plants

Flavanone Glycoside Biosynthesis in Citrus

High Performance Liquid Chromatography and Photodiode Array Detection of Phenylpropanoids and Benzoates inRubus Protoplasts Elicited by Kinetin

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