Dimethylallylpyrophosphate:3,9‐dihydroxypterocarpan 10‐dimethylallyl transferase from <i>Phaseolus vulgaris</i> Identification of the reaction product and properties of the enzyme

Biggs, David R.; Welle, Roland; Visser, Frans R.; Grisebach, Hans

doi:10.1016/0014-5793(87)80909-2

Cited by 30 publications

(12 citation statements)

References 12 publications

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“…These receptors may aid in the removal of invading microorganisms Such as yeast. Purified yeast glucan, which is also a branched (1 ---, 3), (1 --* 6)-[3-glucan (Katohda et al 1976), has been shown to be an effective elicitor of phytoalexins in soybean (Hahn and Albersheim 1978) and partially purified yeast glucan has been used in bean to induce a phytoalexin response (Biggs et al 1987) therefore suggesting that other legumes besides soybean may respond to this type of carbohydrate.…”

Section: Discussionmentioning

confidence: 97%

High-affinity binding of fungal ?-glucan elicitors to cell membranes of species of the plant family Fabaceae

Cosio¹,

Feger²,

Miller³

et al. 1996

Planta

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Abstract. Microsomal preparations of six species of the plant family Fabaceae were screened for high-affinity binding of branched (1 ~ 3), (1 --, 6)-[3-glucans. Oligoglucosides of this type are specific elicitors of phytoalexin accumulation in soybean (Glycine max L.), a member of this family. The species studied were alfalfa (Medicago sativa L.), broadbean (Vicia faba L.), chickpea (Cicer arietinum L.), french bean (Phaseolus vulgaris L.), pea (Pisum sativum L.), and white lupin (Lupinus albus L.). A 125I-labeled 4-(2-aminophenyl)ethylamine conjugate of a (1 ~ 3), (1 ~ 6)-[3-glucan fraction with an average degree of polymerization (DP) of 18, obtained from mycelial walls of Phytophthora sojae, was used as radioligand for initial screening. The structural complexity of this fraction allowed the identification of binding sites with affinities for isomeric structures other than the (1 ~ 3), (1--* 6)-hepta-[3-glucoside for which soybean binding sites display highest affinity. Radioligand competition experiments against unlabeled fungal [3-glucan resulted in the identification of high-affinity binding in alfalfa, bean, lupin, and pea. Half-maximal competition concentrations (ICso) for fungal [3-glucan in these species were between 5 and 30 nM. Pseudoheterologous radioligand competition by unlabeled hepta-[3-glucoside showed that for alfalfa, lupin and pea the ICs0 values for this structure (4 to 16 nM) * Present address: Pontificia Universidad Catolica del Peru, Lima 100, Peru ** Present address: Botariisches Institut der Universitfit, D-80638 Miinchen, Germany Abbreviations: DP = degree of polymerization; ECso = concentration of elicitor necessary to obtain a half-maximal biological response; HG = synthetic (1 ~ 3), (1 ~ 6)-hepta-~-glucoside phytoalexin elicitor; HG-APEA = 1-[4-(2-aminophenyl)ethylamino-1-hexaglucosyl]deoxyglucitol; ICso = ligand concentration necessary to obtain half-maximal displacement of radioligand in competition binding assays; Ka = dissociation constant; OS = branched (1 ~ 3), (1-,6)-~-glucan obtained by hydrolysis of mycelial walls of Phytophthora sojae; OS-APEA = 1-[4-(2-aminophenyl)ethylamino-1-oligoglucosyl]deoxyglucitol conjugate of OS Correspondence to: J. Ebel; FAX: 49(89)1782274; E-mail: j.ebel@botanik.biologie.uni-muenchen.de were similar to those of soybean (7.7 nM). Bean microsomes, however, displayed an IC5o significantly higher than soybean (68 nM) suggesting that the structural motif recognized by its binding sites is not identical to that of soybean or the other three species. Radioligand saturation assays with alfalfa, lupin and pea microsomes using an 125i_labele d aminophenylethylamine hepta-[~-glucoside conjugate gave dissociation constants (Ka) of 5.3, 3.7, and 1.8 nM, respectively. The affinity of these sites for hepta-13-glucoside was in the same range as that of soybean (Ka 1-3 nM), whereas the affinity of the binding sites of bean for the same ligand was significantly lower (Ka = 33 nM). Good correlation was found between the presence of high-affinity binding and the a...

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Section: Discussionmentioning

confidence: 97%

High-affinity binding of fungal ?-glucan elicitors to cell membranes of species of the plant family Fabaceae

Cosio¹,

Feger²,

Miller³

et al. 1996

Planta

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“…For example, methoxy or methylenedioxy groups at C-4# (isoflavone numbering) are the characteristic features of phytoalexins of pea (Pisum sativum), alfalfa, and licorice (Tahara and Ibrahim, 1995;Dixon, 1999). Another typical modification of the isoflavonoid skeleton is prenylation in the phytoalexins of soybean, bean (Phaseolus vulgaris), and lupin (Lupinus albus; Schröder et al, 1979;Biggs et al, 1987;Laflamme et al, 1993). However, the molecular basis of the prenyl transfer reaction onto the isoflavonoid skeleton has not been determined previously.…”

Section: Discussion Prenylation As a Typical Modification Of Flavonoidsmentioning

confidence: 99%

“…In addition, a pterocarpanoid dimethylallyltransferase with different regiospecificity (3,9-dihydroxypterocarpan 10-dimethylallyltransferase) has been characterized in bean (Biggs et al, 1987). A large family of isoflavonoid prenyltransferases can thus be envisaged.…”

Section: Prenyltransferase Family Accepting Aromatic Substratesmentioning

confidence: 99%

Molecular Cloning and Characterization of a cDNA for Pterocarpan 4-Dimethylallyltransferase Catalyzing the Key Prenylation Step in the Biosynthesis of Glyceollin, a Soybean Phytoalexin

et al. 2008

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Glyceollins are soybean (Glycine max) phytoalexins possessing pterocarpanoid skeletons with cyclic ether decoration originating from a C5 prenyl moiety. Enzymes involved in glyceollin biosynthesis have been thoroughly characterized during the early era of modern plant biochemistry, and many genes encoding enzymes of isoflavonoid biosynthesis have been cloned, but some genes for later biosynthetic steps are still unidentified. In particular, the prenyltransferase responsible for the addition of the dimethylallyl chain to pterocarpan has drawn a large amount of attention from many researchers due to the crucial coupling process of the polyphenol core and isoprenoid moiety. This study narrowed down the candidate genes to three soybean expressed sequence tag sequences homologous to genes encoding homogentisate phytyltransferase of the tocopherol biosynthetic pathway and identified among them a cDNA encoding dimethylallyl diphosphate: (6aS, 11aS)-3,9,6a-trihydroxypterocarpan [(−)-glycinol] 4-dimethylallyltransferase (G4DT) yielding the direct precursor of glyceollin I. The full-length cDNA encoding a protein led by a plastid targeting signal sequence was isolated from young soybean seedlings, and the catalytic function of the gene product was verified using recombinant yeast microsomes. Expression of the G4DT gene was strongly up-regulated in 5 to 24 h after elicitation of phytoalexin biosynthesis in cultured soybean cells similarly to genes associated with isoflavonoid pathway. The prenyl part of glyceollin I was demonstrated to originate from the methylerythritol pathway by a tracer experiment using [1-13C]Glc and nuclear magnetic resonance measurement, which coincided with the presumed plastid localization of G4DT. The first identification of a pterocarpan-specific prenyltransferase provides new insights into plant secondary metabolism and in particular those reactions involved in the disease resistance mechanism of soybean as the penultimate gene of glyceollin biosynthesis.

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“…Prenyltransferases catalysing the transfer of a 5-carbon dimethylallyl moiety from dimethylallylpyrophosphate to acceptor isoflavonoids have been reported and partially characterised from soybean (Zfihringer et al 1981), bean (Biggs et al 1987) and lupin (Schr6der et al 1979). It is now well established that the other particulate enzymes of isoflavonoid biosynthesis from soybean: cinnamic acid 4-monooxygenase, isoflavone synthase, pterocarpan 6a-hydroxylase and glyceollidin cyclase, are associated with the endoplasmic reticulum (Kochs and Grisebach 1986;Welle and Grisebach 1988).…”

Section: Introductionmentioning

confidence: 96%

“…In Ruta graveolens, an analogous enzyme catalysing the prenylation of umbelliferone to demethylsuberosin as the first step in furanocoumarin biosynthesis seems to be located in the chloroplasts (Dhillon and Brown 1976). In connection with work on the bean prenyltransferase (Biggs et al 1987), with the final goal to transfer its gene to white clover, it was important to know the intracellular localization of this enzyme.…”

Section: Introductionmentioning

confidence: 98%

Intracellular localization of prenyltransferases of isoflavonoid phytoalexin biosynthesis in bean and soybean

Biggs

Welle

Grisebach

1990

Planta

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The intracellular localization of prenyltransferases involved in the biosynthesis of the phytoalexins glyceollin in soybean (Glycine max L.) and phaseollin in French bean (Phaseolus vulgaris L.) has been investigated. By sucrose- and Percoll-gradient centrifugation of microsomes of an elicitor-challenged soybean cell culture, the membranes containing prenyltransferase were separated from the endoplasmic reticulum and shown to be lighter in density. In a continuous Percoll gradient the peak of prenyltransferase activity coincided with the peak of galactolipid synthesis, as determined by incorporation of uridine 5'-diphospho-[(14)C]galactose (UDP-[(14)C]galactose). Intact chloroplasts isolated from cupricchloride-treated bean leaves contained both prenyltransferase and UDP-galactose transferase activity. Both activities increased during chloroplast isolation. Fractionation of swollen chloroplasts on a discontinuous sucrose gradient showed prenyltransferase and UDP-galactose transferase activity in the envelope membrane subfraction. It is concluded that in both plants prenyltransferase is located in the envelope membrane of plastids.

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Dimethylallylpyrophosphate:3,9‐dihydroxypterocarpan 10‐dimethylallyl transferase from Phaseolus vulgaris Identification of the reaction product and properties of the enzyme

Cited by 30 publications

References 12 publications

High-affinity binding of fungal ?-glucan elicitors to cell membranes of species of the plant family Fabaceae

High-affinity binding of fungal ?-glucan elicitors to cell membranes of species of the plant family Fabaceae

Molecular Cloning and Characterization of a cDNA for Pterocarpan 4-Dimethylallyltransferase Catalyzing the Key Prenylation Step in the Biosynthesis of Glyceollin, a Soybean Phytoalexin

Intracellular localization of prenyltransferases of isoflavonoid phytoalexin biosynthesis in bean and soybean

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