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Flavone glucoside uptake into barley mesophyll and Arabidopsis cell culture vacuoles. Energization occurs by H(+)-antiport and ATP-binding cassette-type mechanisms.

In many cases, secondary plant products accumulate in the large central vacuole of plant cells. However, the mechanisms involved in the transport of secondary compounds are only poorly understood. Here, we demonstrate that the transport mechanisms for the major barley (Hordeum vulgare) flavonoid saponarin (apigenin 6-C-glucosyl-7-O-glucoside) are different in various plant species: Uptake into barley vacuoles occurs via a proton antiport and is competitively inhibited by isovitexin (apigenin 6-C-glucoside), suggesting that both flavone glucosides are recognized by the same transporter. In contrast, the transport into vacuoles from Arabidopsis, which does not synthesize flavone glucosides, displays typical characteristics of ATP-binding cassette transporters. Transport of saponarin into vacuoles of both the species is saturable with a K(m) of 50 to 100 microM. Furthermore, the uptake of saponarin into vacuoles from a barley mutant exhibiting a strongly reduced flavone glucoside biosynthesis is drastically decreased when compared with the parent variety. Thus, the barley vacuolar flavone glucoside/H(+) antiporter could be modulated by the availability of the substrate. We propose that different vacuolar transporters may be responsible for the sequestration of species-specific/endogenous and nonspecific/xenobiotic secondary compounds in planta.

ATP-Binding Cassette Transporters↗

Structure-activity relationships of oligo-beta-glucoside elicitors of phytoalexin accumulation in soybean.

The abilities of a family of chemically synthesized oligo-beta-glucosides, ranging in size from hexamer to decamer, to induce phytoalexin accumulation in soybean cotyledons were investigated to determine which structural elements of the oligoglucosides are important for their biological activity. The results of the biological assays established that the following structural motif is necessary for the oligo-beta-glucosides to have high elicitor activity: [formula; see text] The branched trisaccharide at the nonreducing end of the oligoglucosides was found to be essential for maximum elicitor activity. Substitution of either the nonreducing terminal backbone glucosyl residue or the side-chain glucosyl residue closest to the nonreducing end with glucosaminyl or N-acetylglucosaminyl residues reduced the elicitor activity of the oligoglucosides between 10-fold and 10,000-fold. Elicitor activity was also reduced 1000-fold if the two side-chain glucosyl residues were attached to adjacent backbone glucosyl residues rather than to glucosyl residues separated by an unbranched residue. In contrast, modifications of the reducing terminal glucosyl residue of an elicitor-active hepta-beta-glucoside by conjugation with tyramine and subsequent iodination had no significant effect on the elicitor activity of the hepta-beta-glucoside. These results demonstrate that oligo-beta-glucosides must have a specific structure to trigger the signal transduction pathway, which ultimately leads to the de novo synthesis of phytoalexins in soybean.

Carbohydrate Conformation↗

The glucosyltransferase UGT72E2 is responsible for monolignol 4-O-glucoside production in Arabidopsis thaliana.

The phenylpropanoid pathway in plants leads to the synthesis of a wide range of soluble secondary metabolites, many of which accumulate as glycosides. In Arabidopsis, a small cluster of three closely related genes, UGT72E1-E3, encode glycosyltransferases shown to glucosylate several phenylpropanoids in vitro, including monolignols, hydroxycinnamic acids and hydroxycinnamic aldehydes. The role of these genes in planta has now been investigated through genetically downregulating the expression of individual genes or silencing the entire cluster. Analysis of these transgenic Arabidopsis plants showed that the levels of coniferyl and sinapyl alcohol 4-O-glucosides that accumulate in light-grown roots were significantly reduced. A 50% reduction in both glucosides was observed in plants in which UGT72E2 was downregulated, whereas silencing the three genes led to a 90% reduction, suggesting some redundancy of function within the cluster. The gene encoding UGT72E2 was constitutively overexpressed in transgenic Arabidopsis to determine whether increased glucosylation of monolignols could influence flux through the soluble phenylpropanoid pathway. Elevated expression of UGT72E2 led to increased accumulation of monolignol glucosides in root tissues and also the appearance of these glucosides in leaves. In particular, coniferyl alcohol 4-O-glucoside accumulated to massive amounts (10 micromol g(-1) FW) in root tissues of these plants. Increased glucosylation of other phenylpropanoids also occurred in plants overexpressing this glycosyltransferase. Significantly changing the pattern of glycosides in the leaves also led to a pronounced change in accumulation of the hydroxycinnamic ester sinapoyl malate. The data demonstrate the plasticity of phenylpropanoid metabolism and the important role that glucosylation of secondary metabolites can play in cellular homeostasis.

Arabidopsis↗

Morphogenesis and differentiation of Dictyostelium cells interacting with immobilized glucosides: dependence on DIF production.

Previous work has shown that multicellular morphogenesis of submerged Dictyostelium cells is inhibited when they bind to glucosides covalently linked to polyacrylamide gels. The amoebae aggregate normally, but then the aggregates repeatedly disperse and reaggregate, whereas control cells go on to form tight aggregates. We have investigated the role of the stalk cell differentiation inducing factors (DIFs) in this process. In the presence of cyclic AMP, amoebae submerged at high cell density accumulate DIF and differentiate into stalk cells. We find that stalk cell differentiation is inhibited by interaction of the cells with glucoside gels in these conditions, but can be restored by the addition of exogenous DIF-1. Since the responsiveness of cells to DIF-1 is not altered, it appears likely that the effect of the glucoside gel is to block DIF-1 production. Further, the addition of DIF-1 or DIF-2 stimulates the formation of tight aggregates by cells developing on glucoside gels in the absence of cyclic AMP, thus preventing the rounds of aggregation and disaggregation otherwise seen. This suggests a role for DIF in morphogenesis as well as in controlling cell differentiation. We propose a model in which immobilized glucosides activate a specific receptor ("food sensor") which drives the amoebae toward the vegetative state and inhibits DIF accumulation. DIF, on the other hand, induces tight aggregate formation and so locks the amoebae into the developmental program.

Animals↗

Metabolic profile of FYX-051 (4-(5-pyridin-4-yl-1h-[1,2,4]triazol-3-yl)pyridine-2-carbonitrile) in the rat, dog, monkey, and human: identification of N-glucuronides and N-glucosides.

FYX-051, 4-(5-pyridin-4-yl-1H-[1,2,4]triazol-3-yl)pyridine-2-carbonitrile, is a novel xanthine oxidoreductase inhibitor that can be used for the treatment of gout and hyperuricemia. We examined the metabolism of FYX-051 in rats, dogs, monkeys, and human volunteers after the p.o. administration of this inhibitor. The main metabolites in urine were pyridine N-oxide in rats, triazole N-glucoside in dogs, and triazole N-glucuronide in monkeys and humans, respectively. Furthermore, N-glucuronidation and N-glucosidation were characterized by two types of conjugation: triazole N(1)- and N(2)-glucuronidation and N(1)- and N(2)-glucosidation, respectively. N(1)- and N(2)-glucuronidation was observed in each species, whereas N(1)- and N(2)-glucosidation was mainly observed in dogs. With regard to the position of conjugation, N(1)-conjugation was predominant; this resulted in a considerably higher amount of N(1)-conjugate in each species than N(2)-conjugate. The present results indicate that the conjugation reaction observed in FYX-051 metabolism is unique, i.e., N-glucuronidation and N-glucosidation occur at the same position of the triazole ring, resulting in the generation of four different conjugates in mammals. In addition, a urinary profile of FYX-051 metabolites in monkeys and humans was relatively similar; triazole N-glucuronides were mainly excreted in urine.

Animals↗

New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog.

The Bacillus subtilis sacY and sacT genes encode antiterminator proteins, similar to the Escherichia coli bglG gene product and required for transcription of sucrose metabolism genes. A Tn10 insertion into bglP (formerly sytA) has been previously identified as restoring sucrose utilization to a strain with deletions of both sacY and sacT. The nucleotide sequence of bglP showed a high degree of homology with the E. coli bglF gene (BglF is a beta-glucoside permease of the phosphotransferase system and also acts as a negative regulator of the BglG antiterminator). Complementation studies of an E. coli strain with a deletion of the bgl operon showed that BglP was a functional beta-glucoside permease. In B. subtilis, bglP complemented in trans both the bglP::Tn10 original insertion and a phenotypically similar bglP deletion. Disruption of licT abolished the suppressor phenotype in a bglP mutant. LicT is a recently identified third B. subtilis antiterminator of the BglG/SacY family. These observations indicated that BglP was also a negative regulator of LicT. Both LicT and BglP seem to be involved in the induction by beta-glucosides of an operon containing at least two genes, bglP itself and bglH, encoding a phospho-beta-glucosidase. Other beta-glucoside genes homologous to bglP and bglH have been recently described in B. subtilis. Thus, B. subtilis possesses several sets of beta-glucoside genes, like E. coli, but these genes do not appear to be cryptic.

Amino Acid Sequence↗

Analysis of Ginkgo biloba for the presence of ginkgotoxin and ginkgotoxin 5'-glucoside.

Hot water extracts of Ginkgo biloba seeds were analyzed for the presence of ginkgotoxin (4'-O-methylpyridoxine) by reversed-phase liquid chromatography (LC) using methanol-0.05M KH2PO4 (1 + 9, v/v) adjusted to pH 3 as mobile phase. Detection was by fluorescence (excitation 280 nm, emission 370 nm). A straight line calibration curve was obtained for the 10-100 ng injected. After addition of beta-glucosidase (37 degrees C/h), an earlier eluting peak disappeared and the ginkgotoxin peak increased. The identity of the ginkgotoxin was confirmed by LC/MS and LC/MS/MS. LC/MS/MS also confirmed the 5'-glucoside by comparison with the 3-glucoside. This is the first identification of a glucoside of ginkgotoxin in Ginkgo biloba. An unknown compound of MW 267 also observed in the Ginkgo biloba seed extract was shown not to be 3,5'-diacetylginkgotoxin by its different LC retention time. Extraction of ground Ginkgo biloba seeds with boiling water in a Soxhlet for 2 x 2 h yielded a total of 179 microg/g of free ginkgotoxin. The concentration in powder from Ginkgo biloba capsules was several times lower than this (17-64 microg/g) in 3 samples but higher in another (457 microg/g). Canned ginkgo seeds (white nuts) contained no detectable free ginkgotoxin but the glucoside was present. Different extraction times were studied: 0.5 h gave only 52 microg/g free ginkgotoxin in the ginkgo seeds. However, boiling an extract for 4 h showed about 15% loss of ginkgotoxin and its glucoside.

Chromatography, Liquid↗

[Screening for limonoid glucosides in Citrus grandis L. Osbeck by high performance liquid chromatography-electrospray ionization/mass spectrometry].

A screening method for limonoid glucosides in the peel of Citrus grandis L. Osbeck, utilizing high performance liquid chromatography (HPLC) with diode-array detection (DAD), interfaced to electrospray ionization-mass spectrometry (ESI-MS), has been developed. The methanol extract of citrus peel was preseparated with conventional polymer adsorption column and weak base anion ion-exchange column and then the eluate from the column was analysed by LC-ESI/MS. In this paper, the UV-Vis spectra and the mass spectra provide structural information without the necessity of isolating the individual compounds. Two major limonoid glucosides-obacunone glucoside (OG) and nomilin glucoside (NG) were identified in the methanol extract of the peel of Citrus grandis L. Osbeck. Then the two limonoid glucosides were taken as the target and isolated by means of preparative HPLC on a C18 reversed-phase column with an acidic acetonitrile-water mobile phase. The structures of OG and NG were further confirmed by NMR spectrometry. The results show that this method is rapid, convenient, sensitive and very useful for screening bioactive natural products.

Chromatography, High Pressure Liquid↗

[Research on the separation of limonoid glucosides by reversed-phase preparative high performance liquid chromatography].

Obacunone-17-beta-D-glucopyranoside (OG) was isolated from the seeds of Citrus Sinensis Osbeck by using solvent extraction, classical polymer adsorption column separation and weak base anion ion-exchange separation, OG was finally purified by C18 reversed-phase preparative high performance liquid chromatography and was identified by thin-layer chromatography. The purity of OG was analyzed by analytical reversed-phase HPLC. At last the structure of OG was determined by 1H and 13C nuclear magnetic resonance spectrometry (NMR). In this work, the conditions of the reversed-phase preparative HPLC technique to purify limonoid glucosides was optimized. The reversed-phase preparative HPLC on a C18 column with a mobile phase of acidic acetonitrile-water (about 0.2% TFA, V/V) at pH 3 enabled the baseline separation of limonoid glucosides in the extract. The results show that OG is the predominant limonoid glucoside in the seeds of Citrus Sinensis Osbeck and nomilin glucoside is the second one. The results also show that the classical polymer adsorption column separation and weak base anion ion-exchange separation are effective for purifying limonoid glucosides.

Chromatography, High Pressure Liquid↗

Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases.

We investigated enzymes participating in alpha-glucoside formation, a novel metabolic pathway of xenobiotics in a metabolic study of indeloxazine hydrochloride in rats. When rat tissue homogenates and the indeloxazine metabolite trans-4-(2-morpholinylmethoxy)-1,2-indandiol (M-2) were incubated, M-2-alpha-glucoside formation was observed in liver. This reaction was almost completely inhibited by the alpha-glucosidase inhibitor acarbose. The liver homogenate was then separated into subcellular fractions and an acid alpha-glucosidase in lysosomes and two neutral alpha-glucosidases in microsomes and cytosol were partially purified. The chromatographic behavior and optimum pH of the glucosyltransferase activity of each of the enzyme preparations were almost identical with those of alpha-glucosidase (hydrolase) activity of the same specimen, suggesting the former activity to be also due to alpha-glucosidase. Agreeing with their hydrolytic substrate specificities, the acid enzyme transferred glucose to M-2 from a series of glucose derivatives, ranging from low molecular maltosaccharides to high molecular glycogen, whereas the neutral enzymes took only low molecular maltosaccharides as glucosyl donors. These results led to the conclusion that the formation of alpha-glucoside conjugates is catalyzed by more than one alpha-glucosidase in the liver and uses maltosaccharides or glycogen as glucosyl donors. Several other diol structure-bearing compounds were found in vitro to give rise to alpha-glucoside conjugates, and the mechanism of alpha-glucoside formation is discussed.

Animals↗

A novel UDP-Glc-specific glucosyltransferase catalyzing the biosynthesis of 6-O-glucosides of bile acids in human liver microsomes.

Two active site-directed photoaffinity analogs, 5-[beta-32P]azido-UDP-glucuronic acid and 5-[beta-32P]azido-UDP-glucose, were used for the characterization of UDP-sugar-utilizing enzymes in human liver microsomes. Both compounds were recognized by human microsomal proteins: major photolabeled bands of 50-56 kDa were detected. Both photoincorporations were competitively decreased by increasing concentrations of either UDP-Glc or UDP-GlcUA, indicating a high affinity for both nucleotides. The patterns of photoaffinity labeling in the 50-56-kDa range by the two probes were significantly different, indicating the presence of different UDP-GlcUA- and UDP-Glc-specific enzymes of similar molecular mass. The presence of a UDP-Glc-dependent transferase was confirmed by the identification of an enzymatic activity catalyzing the formation of glucosides of the 6 alpha-hydroxylated bile acid hyodeoxycholic acid (3 alpha, 6 alpha-diOH (HDCA)) in the presence of UDP-Glc. The specific activity of 1.5-3.2 nmol/min/mg of protein was similar to that of 6 alpha-glucuronidation of HDCA. The apparent Km for UDP-Glc estimated with HDCA was 280 microM, and the formation of HDCA glucosides was strongly inhibited by UDP-GlcUA (apparent Ki = 7 microM). Evidence is presented that HDCA-specific UDP-glucuronosyltransferase (clone UGT2B4) expressed in V79 cells is not involved in glucosidation of HDCA and is not photolabeled with 5-[beta-32P]azido-UDP-Glc. Rigorous structure identification of the biosynthetic product proved that HDCA was glucosidated at the 6-position. Thus, this UDP-Glc-dependent activity catalyzing the biosynthesis of 6-O-glucosides of 6 alpha-hydroxylated bile acids represents a new pathway in the metabolism of these bile acids.

Adolescent↗

Antitumour and immunosuppressive activity of hydroxyanthraquinones and their glucosides.

Both isomeric monohydroxyanthraquinones (1a, b), three dihydroxyanthraquinones (alizarin 1c, chrysazin 1d, and anthraflavin 1e) and corresponding acetylated (2) and free (3) beta-D-glucosides were screened for antitumour and immunosuppressive activity. Furthermore, four O-acetyl and O-benzyl derivatives of alizarin (5a--d) were tested. Antitumour activity was judged by the inhibition of growth of syngeneic tumours in the treated recipients and immunosuppressive activity by the effect on tumour growth or on skin graft survival in pretreated allogeneic recipients; as standard of reference served the activity of certain cancerostatic or immunosuppressive drugs used in clinical practice. 1-Hydroxyanthraquinone (1a), alizarin (1c), chrysazin (1d), acetylated glucoside of 2-hydroxyanthraquinone (2b), 2-benzylalizarin (5c), and 1-acetyl-2-benzylalizarin (5d) were found to exhibit antitumour activity. Distinct immunosuppressive activity was detected in alizarin (1c), acetylated glucoside of 1-hydroxyanthraquinone (2a), acetylated glucoside of 2-hydroxyanthraquinone (2b), acetylated glucoside of chrysazin (2d), 2-acetylalizarin (5a), and 1-acetyl-2-benzylalizarin (5d). The group of hydroxyanthraquinone glucodises (3a--3d) exhibited neither antitumour nor immunosuppressive activity.

Animals↗

Malonyl-coenzyme A:isoflavone 7-O-glucoside-6"-O-malonyltransferase from roots of chick pea (Cicer arietinum L.).

A malonyltransferase which catalyzes the malonylation of isoflavone 7-O-glucosides in position 6 of the glucose moiety using malonyl-coenzyme A as acyl donor has been purified 157-fold from 4-day-old roots of chick pea (Cicer arietinum L.). The enzyme showed a pH optimum of 8.0 and a molecular weight of 112,000. The Km for malonylcoenzyme A was 48 microM and, for the chick pea isoflavones biochanin A and formononetin, 36 and 24 microM, respectively. Various other isoflavone, flavone, and flavonol 7-O-glucosides and chalcone 4'-O-glucosides were much poorer substrates. Flavonol 3-O-glucosides and isoflavone 4'-O-glucosides were not malonylated by the malonyltransferase.

Acyl Coenzyme A↗

Characterization of beta-glucosidases with high specificity for the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) moench seedlings.

Two beta-glucosidases exhibiting high specificity for the cyanogenic glucoside dhurrin have been purified to near homogeneity from seedlings of Sorghum bicolor. Dhurrinase 1 was isolated from shoots of seedlings grown in the dark. Dhurrinase 2 was isolated from the green shoots of young seedlings grown in the light. The two enzymes were similar in following characteristics: their optimum activity is around pH 6.2; the enzymes are stable above pH 7; they are effectively inhibited by the beta-glycosidase inhibitors nojirimycin delta-gluconolactone and 1-amino-beta-D-glucoside. On the other hand, they clearly differed in other properties, e.g., molecular weights, isoelectric points, and substrate specificity. Moreover, dithiothreitol has no effect on dhurrinase 1, but is necessary for the activity of dhurrinase 2. Preliminary investigations indicate that the two enzymes are located in different parts of the sorghum seedlings: dhurrinase 1 is found in the coleoptiles and hypocotyls; dhurrinase 2 occurs in the leaves. Dhurrin (p-hydroxy-(S)-mandelonitrile-beta-D-glucoside) and its structural analog without the hydroxyl group, sambunigrin, were the only substrates hydrolyzed at high rate, the Km values with both enzymes being 0.15 and 0.3 mM, respectively. All other cyanogenic glucosides tested, as well as synthetic substrates such as 4-nitrophenyl-beta-D-glucoside, were in general poor substrates, especially for dhurrinase 1, the enzyme isolated from coleoptile and hypocotyl tissue. Dhurrinase 1 appears to exist within the seedlings as a tetramer (Mr - 2-2.4 X 10(5)) which dissociates without loss of activity into a dimeric form (Mr = 1-1.1 X 10(5)) upon extraction and purification. There is only one monomeric subunit with Mr = 5.7 X 10(4). Isolectric focusing and chromatofocusing of purified dhurrinase 1 showed the presence of at least three isomeric forms, but their relationship to each other is not known at the present time. Dhurrinase 2 appears to be a tetrameric protein with Mr = 2.5-3 X 10(5); it also has only one monomeric subunit of Mr = 6.1 X 10(4). In contrast to many other beta-glucosidases, the dhurrinases are not glycoproteins.

Dithiothreitol↗

The effect of azaserine upon the proline and methyl alpha-D-glucoside transport systems of rat renal brush-border membranes.

An inhibitory effect of azaserine on Na+ dependent proline and methyl alpha-D-glucoside transport of the rat renal brush-border membrane vesicles has been demonstrated. The inhibitory effects of azaserine were not the results of the drug disrupting the membrane vesicles as shown in osmolarity studies, nor did it affect the transport systems' affinities for Na+. Azaserine acts as a non-competitive inhibitor for the proline transport system in renal brush-border membranes by lowering 37% and 27% in the Vmax1 and Vmax2, respectively, when compared to that of control proline transport system. Azaserine had no effect upon the two Km values for proline uptake. Azaserine inhibition of methyl alpha-D-glucoside uptake by vesicles in the presence of 7.2 mM azaserine at 22 degrees C resulted in 66% increase in Km1 value and 44% decrease in Vmax1 as compared to that of control vesicles. There was no detectable effect upon the Km2 and Vmax2 of the methyl alpha-D-glucoside transport system. No effect of the drug was observed when sodium was equilibrated across the membrane, indicating that azaserine altered the driving force exerted by a sodium gradient. Azaserine only slightly affected the relative contribution of the two Km systems to total proline uptake. Contrary to the observed effect of azaserine upon the proline transport system, azaserine exerted a distinct effect upon the relative contribution to total uptake by the two Km systems in the low methyl alpha-D-glucoside concentration range. In the presence of 7.2 mM azaserine, the low-affinity, high-Km transport system becomes the major contributor to total methyl alpha-D-glucoside uptake by isolated renal brush-border vesicles.

Animals↗

Cycad toxins, Helicobacter pylori and parkinsonism: cholesterol glucosides as the common denomenator.

Understanding sporadic cases of age-dependent neurodegenerative diseases such as parkinsonism requires the evaluation of potential environmental factors. Amyotrophic lateral sclerosis-parkinsonism dementia complex (ALS-PDC), a neurological disorder in which features of parkinsonism are present and for which no consistent genetic explanation has been found, has been linked to the consumption of cycad (Cycas micronesica). Similarly, epidemiological evidence suggests an association between parkinsonism and gastric ulcer caused by Helicobacter pylori infection. While common immunological and inflammatory changes have been proposed to account for the link between parkinsonism and H. pylori infection, we propose an alternate explanation based on our work on the "cycad theory" of ALS-PDC. Recent experiments in our laboratory have identified several sterol glucosides in cycad that have neurotoxic properties in vitro and that appear to be linked to the development of neurodegenerative disease in vivo. Specifically, mice fed cycad display behavioural symptoms of parkinsonism such as reduced gait length, as well as neuropathological signs such as a loss of striatal dopaminergic (DAergic) terminals and an upregulation of the dopamine D2 receptor. These cycad-derived sterol glucosides are structurally similar to cholesterol glucosides that account for a significant part pf the lipid profile of H. pylori. We hypothesize that cholesterol glucosides arising from H. pylori infection may act as neurotoxins, promoting the degeneration of the DAergic neurons affected in parkinsonism, in a similar reaction to that which is thought to link cycad consumption and ALS-PDC. This hypothesis will be tested in future studies that will include exposing mice to purified sterol or cholestorol glucosides derived from cycad and comparing these mice behaviourally and neuropathologically to ones chronically infected with H. pylori.

Amyotrophic Lateral Sclerosis↗

Cyanogenic glucosides and plant-insect interactions.

Cyanogenic glucosides are phytoanticipins known to be present in more than 2500 plant species. They are considered to have an important role in plant defense against herbivores due to bitter taste and release of toxic hydrogen cyanide upon tissue disruption. Some specialized herbivores, especially insects, preferentially feed on cyanogenic plants. Such herbivores have acquired the ability to metabolize cyanogenic glucosides or to sequester them for use in their predator defense. A few species of Arthropoda (within Diplopoda, Chilopoda, Insecta) are able to de novo synthesize cyanogenic glucosides and, in addition, some of these species are able to sequester cyanogenic glucosides from their host plant (Zygaenidae). Evolutionary aspects of these unique plant-insect interactions with focus on the enzyme systems involved in synthesis and degradation of cyanogenic glucosides are discussed.

Animals↗

Evidence for the direct 2beta- and 3beta-hydroxylation of [2H2]GA20-13-O-[6'-2H2]glucoside in seedlings of Phaseolus coccineus.

[17-2H2]GA20-13-O-[6'-2H2]glucoside was synthesized and applied to seedlings of Phaseolus coccineus L. After incubation for 72 h the conjugate metabolites were purified and shown by LC-ESI-tandem-MS and GC-MS to be [17-2H2]GA1-13-O-[6'-2H2]glucoside and [17-2H2]GA29-13-O-[6'-2H2]glucoside. This is the first evidence for the conversion of intact GA-O-glucosides, and represents an additional metabolic pathway of the gibberellin metabolism in P. coccineus L. The results indicate that intact GA-O-glucosides are accepted by 2- and 3-oxidases in the plant.

Journal Article↗