Strictosidine: a key intermediate in the biogenesis of indole alkaloids

Smith, G. N.

doi:10.1039/c19680000912

Cited by 26 publications

(41 citation statements)

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“…Recent work in this laboratory [3-51 has demonstrated that, unlike previous findings [20,21] it is not vincoside, with the 3-P(R) configuration, but rather its epimer 3-m(S)-strictosidine [22] that is the universal [7,8] biosynthetic precursor for the vast majority of monoterpenoid indole alkaloids. This result was made possible by using cell-free extracts of C. roseus cell suspension cultures which produced substantial amounts of indole alkaloids 193.…”

Section: Discussionmentioning

confidence: 96%

“…On the basis of this and previous [3][4][5]7,8] results we are entitled now to assume that the previously reported natural occurrence of vincoside in Catharanthus roseus [20,27] is either an error or a chemical artefact during feeding or work-up. The alkaloidal glucoside strictosidine isolated and characterized by G. N. Smith [22] is indeed the key intermediate in monoterpene indole alkaloid biosynthesis, as he had already assumed in 1968.…”

Section: Discussionmentioning

confidence: 96%

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Purification and Properties of Strictosidine Synthase, the Key Enzyme in Indole Alkaloid Formation

Treimer

Zenk

1979

European Journal of Biochemistry

166

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A new enzyme, strictosidine synthase, which catalyzes the synthesis of 3-a(S)-strictosidine from tryptamine and secologanin was isolated from the soluble protein extract of Catharanthus roseus cell suspension cultures and was purified approximately 50-fold by ammonium sulfate fractionation, column chromatography on DEAE-cellulose, Ultrogel AcA34 and isoelectric focusing. The apparent molecular weight of the enzyme was 34000. The pH optimum was 6.8, apparent K, values for tryptamine and secologanin were 2.3 mM and 3.4 mM respectively for the enzyme to synthesize strictosidine. Strictosidine synthase shows high substrate specificity. No apparent cofactor requirement could be demonstrated. Of several enzyme inhibitors tested, only p-chloromercuribenzoate inhibited the enzyme. The enzyme was relatively stable and could be stored at -20 "C for periods of up to 1 year without appreciable loss of catalytic activity. The enzyme was demonstrated to occur in suspension cultures of 15 different species belonging to 9 different genera of the indole-alkaloidproducing subfamily Plumerioideae of the Apocynaceae family.This enzyme is responsible for the synthesis of strictosidine the key intermediate in the formation of the majority of monoterpenoid indole alkaloids occurring in the plant kingdom.The indole alkaloids, of which about 1200 are known to date [l], make up the largest class of alkaloids. They comprise such chemically diverse structures as ajmaline, gelsemine, quinine, strychnine, vinblastine etc. By feeding experiments in vivo, it was shown that most of the monoterpenoid alkaloids are formed through the condensation of the iridoid secologanin with tryptamine (reviewed 121). Recently the key enzyme, catalyzing the stereospecific condensation of tryptamine with secologanin to yield the alkaloidal glucoside strictosidine with 3 -4 9 configuration, was discovered [3 -51 and some properties of the enzyme from crude extracts of cell cultures of alkaloid-producing Apocynaceae plants were preliminarily reported for the first time [6]. Strictosidine is the universal precursor for the multitude of monoterpenoid indole alkaloids both of the 3-c( as well as of the 3-1) series [7,8]. This enzyme catalyzes a PictetSpengler-type reaction between the aldehyde function of secologanin and the amino group of tryptamin as shown in Fig. 1. This cyclisation suggests a Schiff-base formation followed by an electrophilic attack of C-2 of the indole ring. During this attack the hydrogen atom of C-2 of the indole was eliminated, which formed the basis for a convenient and sensitive assay of this enzyme using the ring [2-'H]tryptamine as substrate and analysing the H03H formed for radioactivity [6].In extension of our previous work [6], we have now purified strictosidine synthase from Catharanthus roseus (= Vinca rosea) cell suspension cultures. This

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 96%

Purification and Properties of Strictosidine Synthase, the Key Enzyme in Indole Alkaloid Formation

Treimer

Zenk

1979

European Journal of Biochemistry

166

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“…After the ubiquitous biosynthetic pathway leading to geranyl diphosphate, a series of specific steps restricted to a few plant species lead to secologanin through loganic acid. Secologanin and tryptamine are stereospecifically condensed to strictosidine by strictosidine synthase and further converted to other indole alkaloids such as ajmalicine, catharanthine, or vindoline (Smith, 1968;Scott et al, 1977;Zenk, 1977a, 1977b). The level of loganic acid and secologanin in phytoplasma-infected C. roseus leaves was highly increased, and this increased level is well correlated with those of Glc and Suc.…”

Section: Discussionmentioning

confidence: 99%

Metabolic Discrimination ofCatharanthus roseusLeaves Infected by Phytoplasma Using 1H-NMR Spectroscopy and Multivariate Data Analysis

et al. 2004

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A comprehensive metabolomic profiling of Catharanthus roseus L. G. Don infected by 10 types of phytoplasmas was carried out using one-dimensional and two-dimensional NMR spectroscopy followed by principal component analysis (PCA), an unsupervised clustering method requiring no knowledge of the data set and used to reduce the dimensionality of multivariate data while preserving most of the variance within it. With a combination of these techniques, we were able to identify those metabolites that were present in different levels in phytoplasma-infected C. roseus leaves than in healthy ones. The infection by phytoplasma in C. roseus leaves causes an increase of metabolites related to the biosynthetic pathways of phenylpropanoids or terpenoid indole alkaloids: chlorogenic acid, loganic acid, secologanin, and vindoline. Furthermore, higher abundance of Glc, Glu, polyphenols, succinic acid, and Suc were detected in the phytoplasma-infected leaves. The PCA of the 1 H-NMR signals of healthy and phytoplasma-infected C. roseus leaves shows that these metabolites are major discriminating factors to characterize the phytoplasma-infected C. roseus leaves from healthy ones. Based on the NMR and PCA analysis, it might be suggested that the biosynthetic pathway of terpenoid indole alkaloids, together with that of phenylpropanoids, is stimulated by the infection of phytoplasma.

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“…-The universal role of the glucoalkaloid strictosidine as a precursor of ca. 2,000 structurally diverse monoterpenoid indole alkaloids, some being of high commercial value, has been unequivocally demonstrated [1] [2]. The enzyme responsible for strictosidine synthesis, which occurs by way of a stereoselective PictetSpengler reaction [3] of tryptamine with secologanin, has been discussed in detail [4 -6] and is named strictosidine synthase (STR1, EC 4.3.3.2).…”

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confidence: 99%

Improved Expression of His₆‐Tagged Strictosidine Synthase cDNA for Chemo‐Enzymatic Alkaloid Diversification

Yang

Zou

Zhu

et al. 2010

Chemistry & Biodiversity

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Strictosidine synthase (STR1) catalyzes the stereoselective formation of 3alpha(S)-strictosidine from tryptamine and secologanin. Strictosidine is the key intermediate in the biosynthesis of 2,000 plant monoterpenoid indole alkaloids, and it is a key precursor of enzyme-mediated synthesis of alkaloids. An improved expression system is described which leads to optimized His(6)-STR1 synthesis in Escherichia coli. Optimal production of STR1 was achieved by determining the impact of co-expression of chaperones pG-Tf2 and pG-LJE8. The amount and activity of STR1 was doubled in the presence of chaperone pG-Tf2 alone. His(6)-STR1 immobilized on Ni-NTA can be used for enzymatic synthesis of strictosidines on a preparative scale. With the newly co-expressed His(6)-STR1, novel 3alpha(S)-12-azastrictosidine was obtained by enzymatic catalysis of 7-azatryptamine and secologanin. The results obtained are of significant importance for application to chemo-enzymatic approaches leading to diversification of alkaloids with novel improved structures.

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Strictosidine: a key intermediate in the biogenesis of indole alkaloids

Cited by 26 publications

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Purification and Properties of Strictosidine Synthase, the Key Enzyme in Indole Alkaloid Formation

Purification and Properties of Strictosidine Synthase, the Key Enzyme in Indole Alkaloid Formation

Metabolic Discrimination ofCatharanthus roseusLeaves Infected by Phytoplasma Using 1H-NMR Spectroscopy and Multivariate Data Analysis

Improved Expression of His₆‐Tagged Strictosidine Synthase cDNA for Chemo‐Enzymatic Alkaloid Diversification

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Strictosidine: a key intermediate in the biogenesis of indole alkaloids

Cited by 26 publications

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Purification and Properties of Strictosidine Synthase, the Key Enzyme in Indole Alkaloid Formation

Purification and Properties of Strictosidine Synthase, the Key Enzyme in Indole Alkaloid Formation

Metabolic Discrimination ofCatharanthus roseusLeaves Infected by Phytoplasma Using 1H-NMR Spectroscopy and Multivariate Data Analysis

Improved Expression of His6‐Tagged Strictosidine Synthase cDNA for Chemo‐Enzymatic Alkaloid Diversification

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Improved Expression of His₆‐Tagged Strictosidine Synthase cDNA for Chemo‐Enzymatic Alkaloid Diversification