Substrate specificity in vivo and in vitro in the formation of stilbenes. Biosynthesis of rhaponticin

Rupprich, Norbert; Hildebrand, H.; Kindl, Helmut

doi:10.1016/0003-9861(80)90332-x

Cited by 57 publications

(33 citation statements)

References 16 publications

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“…Stems of 2-week-old plants were excised, cut into pieces, and placed on B5 medium (4) (2). Resveratrol was purified by chromatography in more than one well established solvent system (1,9) and comparison with material isolated from Veratrum album (16). System 2 (for TLC), toluene:methanol (9:1); system 3 (for PC), acetic acid:water (1:2).…”

Section: Methodsmentioning

confidence: 99%

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Stilbene Synthase and Chalcone Synthase

Rolfs¹,

Kindl²

1984

Plant Physiol.

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ABSTlRACFCultured cells of Picea excelsa capable of forming sdlbenes and flavanoids have been established. Unlike needles of intact plants continin piceatannol (3,3',4',5-tetrahydroxystilbene) Stilbene synthase is the key enzyme on the way to fungostatic stilbene derivatives characterized as phytoalexins (6, 8, 1 1). Chalcone synthase initiates the route to a flavanone and thus to other phytoalexins, e.g the one having a pterocarpan skeleton (7). Both enzymes function with the same substrates, malonyl-CoA and pcoumaroyl-CoA, and have in common mechanistic details of catalysis, i.e. nucleophilic attack of anion of acetyl-CoA at the ester group of the aromatic substrate (7, 12, 18). They fold, however, the intermediary polyketide chain topologically in a different way and apply different mechanisms of cyclization.It was, therefore, ofinterest to compare the two enzymes when occurring in the same species. The primary purpose ofthe present study was to determine whether the two catalytic activities were due to a single protein modulated by specific cofactors or to two different proteins.The data presented provide evidence that, although stilbene synthase and chalcone synthase resemble each other in several aspects, they are two proteins not related immunologically.

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Section: Methodsmentioning

confidence: 99%

“…Stilbene synthase (resveratrol-forming) was essentially assayed according to (16 and naringenin (Fig. 1).…”

Section: Methodsmentioning

confidence: 99%

Stilbene Synthase and Chalcone Synthase

Rolfs¹,

Kindl²

1984

Plant Physiol.

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“…Products were extracted with ethyl acetate and chromatographed using the solvent systems L3 and L4. As the orchid enzymes were of a different substrate specificity from those we had found before in Rheum rhaponticum [16], Pinus sylvestris [19], Picea excelsa and Vitaceae [20], all preparations were tested with dihydro-mcoumaroyl-CoA in addition to the various cinnamoyl-CoA derivatives.…”

Section: Enzyme Assaymentioning

confidence: 99%

9,10‐Dihydrophenanthrenes as Phytoalexins of Orchidaceae

Fritzemeier

Kindl

1983

European Journal of Biochemistry

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Hydroxy derivatives of 9,10-dihydrophenanthrenes, orchinol and hircinol, were isolated from bulbs of Orchidaceae which had been induced to accumulate phytoalexins. Incorporation of radioactive precursors, Lphenylalanine and various hydroxycinnamic acids, has been investigated by feeding experiments in vivo. m-Coumaric acid and dihydro-m-coumaric acid were found to be efficiently incorporated into the dihydrophenanthrene derivatives. Dihydro-m-coumaric acid was not only converted into the dihydrophenanthrenes but was also formed from L-phenylalanine in the same tissue; it was thus proved to be an intermediate.The role of dihydro-m-coumaric acid was substantiated by studies in vitro. An active stilbene synthase was detected in enzyme preparations from induced orchid bulbs and assayed with different CoA esters. The enzyme, characterized on the basis of its substrate specificity, selectively converted dihydro-m-coumaroyl-CoA plus malonylCoA into 3,3',5-trihydroxybibenzyl.The role of 3,3',5-trihydroxybibenzyl as physiological intermediate was further corroborated by investigations with intact plants. Both its formation from phenylpropanoids and its conversion into orchinol was demonstrated.The data provided evidence for a biosynthetic sequence originating from L-phenylalanine and leading to 9,lOdihydrophenanthrenes via m-coumaric acid, dihydro-m-coumaric acid, and 3,3',5-trihydroxybibenzyl.

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“…The enzyme was therefore clearly distinguished from the resveratrol synthase which converted p-coumaroylCoA 5 times better than cinnamoyl-CoA into the respective stilbene [9]. These two enzymes are the only examples of stilbene synthases active in vitro.…”

Section: Discussionmentioning

confidence: 99%

“…Recently we could demonstrate stilbene biosynthesis in vitro using a partially purified enzyme preparation from the rhizome of Rheum rhaponticum [8,9]. The enzyme catalyzed the formation of resveratrol(3,5,4'-trihydroxystilbene, see fig.l).…”

Section: Introductionmentioning

confidence: 99%