Molecular Characterization of a Membrane-bound Prenyltransferase Specific for Isoflavone from Sophora flavescens

Sasaki, Kenji; Tsurumaru, Yusuke; Yamamoto, Haruhiko; Yazaki, Kazufumi

doi:10.1074/jbc.m111.244426

Cited by 81 publications

(70 citation statements)

References 42 publications

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“…G4DT, SfN8DT-1, and SfG6DT, as well as isoflavone prenyltransferases previously identified only at the biochemical level, are localized in chloroplasts (Biggs et al, 1990;Sasaki et al, 2008Sasaki et al, , 2011Akashi et al, 2009). Our studies here indicate that LaPT1 is likewise localized to plastids, both with and without chlorophyll, when expressed in Medicago hairy roots.…”

Section: Lapt1 Is a Plastid-localized 5-hydroxyisoflavone 39-prenyltrmentioning

confidence: 99%

“…Previous studies have reported the molecular identification of four flavonoid prenyltransferases, three from S. flavescens (SfN8DT-1, SfG6DT, and SfiLDT) and one from soybean (G4DT; Sasaki et al, 2008Sasaki et al, , 2011Akashi et al, 2009). G4DT transfers a prenyl group to the A-ring of a pterocarpan precursor of the glyceollin phytoalexins, SfN8DT-1 prenylates the flavanone naringenin on the A-ring, and SfG6DT prenylates the isoflavone genistein on the A-ring.…”

Section: Lapt1 Is a Plastid-localized 5-hydroxyisoflavone 39-prenyltrmentioning

confidence: 99%

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Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus

et al. 2012

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Prenylated flavonoids and isoflavonoids possess antimicrobial activity against fungal pathogens of plants. However, only a few plant flavonoid and isoflavonoid prenyltransferase genes have been identified to date. In this study, an isoflavonoid prenyltransferase gene, designated as LaPT1, was identified from white lupin (Lupinus albus). The deduced protein sequence of LaPT1 shared high homologies with known flavonoid and isoflavonoid prenyltransferases. The LaPT1 gene was mainly expressed in roots, a major site for constitutive accumulation of prenylated isoflavones in white lupin. LaPT1 is predicted to be a membrane-bound protein with nine transmembrane regions and conserved functional domains similar to other flavonoid and isoflavonoid prenyltransferases; it has a predicted chloroplast transit peptide and is plastid localized. A microsomal fraction containing recombinant LaPT1 prenylated the isoflavone genistein at the B-ring 39 position to produce isowighteone. The enzyme is also active with 29-hydroxygenistein but has no activity with other flavonoid substrates. The apparent K m of recombinant LaPT1 for the dimethylallyl diphosphate prenyl donor is in a similar range to that of other flavonoid prenyltransferases, but the apparent catalytic efficiency with genistein is considerably higher. Removal of the transit peptide increased the apparent overall activity but also increased the K m . Medicago truncatula hairy roots expressing LaPT1 accumulated isowighteone, a compound that is not naturally produced in this species, indicating a strategy for metabolic engineering of novel antimicrobial compounds in legumes.

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Section: Lapt1 Is a Plastid-localized 5-hydroxyisoflavone 39-prenyltrmentioning

confidence: 99%

Section: Lapt1 Is a Plastid-localized 5-hydroxyisoflavone 39-prenyltrmentioning

confidence: 99%

Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus

et al. 2012

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“…Since then, genes encoding various flavonoid PTs have been identified in Leguminosae (Akashi et al, 2009;Sasaki et al, 2011;Shen et al, 2012). Although other prenylated aromatic compounds, including coumarins, xanthons, phenylpropanoids, and phloroglucinols, have been isolated from many plant species, no gene encoding a PT for those aromatics has been isolated, except for the gene encoding a phloroglucinol-specific enzyme (HlPT1) from hops (Humulus lupulus) and a the recently isolated coumarin dimethylallyltransferase from parsley (Tsurumaru et al, 2010Karamat et al, 2014).…”

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confidence: 99%

Molecular Cloning and Characterization of a Geranyl Diphosphate-Specific Aromatic Prenyltransferase from Lemon

Munakata¹,

Inoue

Koeduka

et al. 2014

Plant Physiology

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Prenyl residues confer divergent biological activities such as antipathogenic and antiherbivorous activities on phenolic compounds, including flavonoids, coumarins, and xanthones. To date, about 1,000 prenylated phenolics have been isolated, with these compounds containing various prenyl residues. However, all currently described plant prenyltransferases (PTs) have been shown specific for dimethylallyl diphosphate as the prenyl donor, while most of the complementary DNAs encoding these genes have been isolated from the Leguminosae. In this study, we describe the identification of a novel PT gene from lemon (Citrus limon), ClPT1, belonging to the homogentisate PT family. This gene encodes a PT that differs from other known PTs, including flavonoid-specific PTs, in polypeptide sequence. This membrane-bound enzyme was specific for geranyl diphosphate as the prenyl donor and coumarin as the prenyl acceptor. Moreover, the gene product was targeted to plastid in plant cells. To our knowledge, this is the novel aromatic PT specific to geranyl diphosphate from citrus species.

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“…The first flavonoid prenyltansferase, SfN8DT-1, was identified in Sophora flavescens cell cultures by Sasaki et al (2008). Subsequently, SfG6DT and SfiLDT, which prenylate genistein to produce wighteone (6-dimethylallylgenistein) and isoliquiritigenin to produce dimethyllylisoliquiritigenin, respectively, were identified in the same species (Sasaki et al, 2011). While SfG6DT prenylates genistein on the A-ring of the isoflavone, LaPT1 isolated from another legume, white lupin (Lupinus albus), catalyzes the prenylation of the B-ring of genistein and 29-hydroxygenistein to form isowighteone (39-dimethylallylgenistein) and luteone (29-hydroxy-39-dimethylallyl-genistein), respectively (Shen et al, 2012).…”

Section: Substrate Specificity Of Resveratrol Prenyltransferasementioning

confidence: 99%

A Stilbenoid-Specific Prenyltransferase Utilizes Dimethylallyl Pyrophosphate from the Plastidic Terpenoid Pathway

et al. 2016

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Prenylated stilbenoids synthesized in some legumes exhibit plant pathogen defense properties and pharmacological activities with potential benefits to human health. Despite their importance, the biosynthetic pathways of these compounds remain to be elucidated. Peanut (Arachis hypogaea) hairy root cultures produce a diverse array of prenylated stilbenoids upon treatment with elicitors. Using metabolic inhibitors of the plastidic and cytosolic isoprenoid biosynthetic pathways, we demonstrated that the prenyl moiety on the prenylated stilbenoids derives from a plastidic pathway. We further characterized, to our knowledge for the first time, a membrane-bound stilbenoid-specific prenyltransferase activity from the microsomal fraction of peanut hairy roots. This microsomal fraction-derived resveratrol 4-dimethylallyl transferase utilizes 3,3-dimethylallyl pyrophosphate as a prenyl donor and prenylates resveratrol to form arachidin-2. It also prenylates pinosylvin to chiricanine A and piceatannol to arachidin-5, a prenylated stilbenoid identified, to our knowledge, for the first time in this study. This prenyltransferase exhibits strict substrate specificity for stilbenoids and does not prenylate flavanone, flavone, or isoflavone backbones, even though it shares several common features with flavonoid-specific prenyltransferases.

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Molecular Characterization of a Membrane-bound Prenyltransferase Specific for Isoflavone from Sophora flavescens

Cited by 81 publications

References 42 publications

Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus

Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus

Molecular Cloning and Characterization of a Geranyl Diphosphate-Specific Aromatic Prenyltransferase from Lemon

A Stilbenoid-Specific Prenyltransferase Utilizes Dimethylallyl Pyrophosphate from the Plastidic Terpenoid Pathway

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