Purification and characterization of coclaurine N-methyltransferase from cultured Coptis japonica cells

Choi, Kum-Boo; Morishige, Takashi; Sato, Fumihiko

doi:10.1016/s0031-9422(00)00481-7

Cited by 72 publications

(74 citation statements)

References 17 publications

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“…The apparent K m values for DMAPP and naringenin were calculated to be 106 mM and 55 mM, respectively. These values coincided with those of the native protein (Yamamoto et al, 2000) and are in a similar range of many other secondary metabolic enzymes (Fujiwara et al, 1998;Choi et al, 2002;Suzuki et al, 2002;Fukuchi-Mizutani et al, 2003;Kim et al, 2006). …”

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confidence: 77%

Cloning and Characterization of Naringenin 8-Prenyltransferase, a Flavonoid-Specific Prenyltransferase of Sophora flavescens

et al. 2008

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Prenylated flavonoids are natural compounds that often represent the active components in various medicinal plants and exhibit beneficial effects on human health. Prenylated flavonoids are hybrid products composed of a flavonoid core mainly attached to either 5-carbon (dimethylallyl) or 10-carbon (geranyl) prenyl groups derived from isoprenoid (terpenoid) metabolism, and the prenyl groups are crucial for their biological activity. Prenylation reactions in vivo are crucial coupling processes of two major metabolic pathways, the shikimate-acetate and isoprenoid pathways, in which these reactions are also known as a rate-limiting step. However, none of the genes responsible for the prenylation of flavonoids has been identified despite more than 30 years of research in this field. We have isolated a prenyltransferase gene from Sophora flavescens, SfN8DT-1, responsible for the prenylation of the flavonoid naringenin at the 8-position, which is specific for flavanones and dimethylallyl diphosphate as substrates. Phylogenetic analysis shows that SfN8DT-1 has the same evolutionary origin as prenyltransferases for vitamin E and plastoquinone. The gene expression of SfN8DT-1 is strictly limited to the root bark where prenylated flavonoids are solely accumulated in planta. The ectopic expression of SfN8DT-1 in Arabidopsis thaliana resulted in the formation of prenylated apigenin, quercetin, and kaempferol, as well as 8-prenylnaringenin. SfN8DT-1 represents the first flavonoid-specific prenyltransferase identified in plants and paves the way for the identification and characterization of further genes responsible for the production of this large and important class of secondary metabolites.The prenylation of aromatic compounds is a major contributor to the diversity of plant secondary metabolites due to differences in prenylation position on the aromatic ring, various lengths of prenyl chain, and further modifications of the prenyl moiety, e.g. cyclization and hydroxylation, resulting in the occurrence of more than 1,000 prenylated compounds in plants (Tahara and Ibrahim, 1995;Barron and Ibrahim, 1996). In particular, prenylated flavonoids in higher plants protect them by exhibiting strong antibacterial and antifungal activities (Sohn et al., 2004). Many prenylated flavonoids have been identified as active components in medicinal plants with biological activities, such as anticancer, anti-androgen, anti-leishmania, and anti-nitric oxide production (De Naeyer et al., 2004;Ahmed-Belkacem et al., 2005;Han et al., 2006). Due to the beneficial effects for human health, prenylated flavonoids are of particular interest as lead compounds for producing new drugs and functional foods. The prenylation of the flavonoid core increases the lipophilicity and the membrane permeability, which is one of the proposed reasons for the enhanced biological activities of prenylated flavonoids (Wang et al., 1997;Maitrejean et al., 2000;Murakami et al., 2000). However, none of the genes responsible for the prenylation reactions has been identified d...

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confidence: 77%

Cloning and Characterization of Naringenin 8-Prenyltransferase, a Flavonoid-Specific Prenyltransferase of Sophora flavescens

et al. 2008

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“…The conversion order was inferred by the substrate preference of the relevant enzymes although recent evidence suggests that the pathway is not linear, but rather operates as a grid (Desgagné-Penix and Facchini 2012). (S)-Norcoclaurine is first converted by norcoclaurine-6-O-methyltransferase (6OMT) to (S)-coclaurine (Morishige et al 2000;Ounaroon et al 2003), which is accepted by coclaurine N-methyltransferase (CNMT) (Choi et al 2001). N-Methylcoclaurine is hydroxylated by (S)-N-methylcoclaurine 3′-hydroxylase (NMCH) (Pauli and Kutchan 1998;Frick et al 2007) to 3′-hydroxy-N-methylcoclaurine, which is converted by 3′-hydroxy-N-methylcoclaurine 4′-O-methyltransferase (4′OMT) (Morishige et al 2000) to (S)-reticuline.…”

Section: Biosynthesis Of the Major Alkaloids In Opium Poppymentioning

confidence: 99%

Benzylisoquinoline alkaloid biosynthesis in opium poppy

Beaudoin

Facchini

2014

Planta

225

161

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“…Benzylisoquinoline alkaloid biosynthetic genes from C. japonica and P. somniferum were used as heterologous probes to isolate cDNAs encoding eight additional protoberberine alkaloid biosynthetic enzymes from T. flavum. Full-length genomic clones encoding 6OMT (Morishige et al, 2000), CNMT (Choi et al, 2002), 49OMT (Morishige et al, 2000), SOMT (Takeshita et al, 1995), CYP80B (Ikezawa et al, 2003), and CYP719A (Ikezawa et al, 2003) were amplified from C. japonica genomic DNA by PCR using gene-specific primers. Genetic sequences encoding TYDC (Facchini and De Luca, 1994) and BBE (Facchini et al, 1996) from P. somniferum were reported previously.…”

Section: Molecular Cloning Of the Protoberberine Alkaloid Pathway Fromentioning

confidence: 99%

Cell Type–Specific Localization of Transcripts Encoding Nine Consecutive Enzymes Involved in Protoberberine Alkaloid Biosynthesis

2005

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Molecular clones encoding nine consecutive biosynthetic enzymes that catalyze the conversion of L-dopa to the protoberberine alkaloid (S)-canadine were isolated from meadow rue (Thalictrum flavum ssp glaucum). The predicted proteins showed extensive sequence identity with corresponding enzymes involved in the biosynthesis of related benzylisoquinoline alkaloids in other species, such as opium poppy (Papaver somniferum). RNA gel blot hybridization analysis showed that gene transcripts for each enzyme were most abundant in rhizomes but were also detected at lower levels in roots and other organs. In situ RNA hybridization analysis revealed the cell type-specific expression of protoberberine alkaloid biosynthetic genes in roots and rhizomes. In roots, gene transcripts for all nine enzymes were localized to immature endodermis, pericycle, and, in some cases, adjacent cortical cells. In rhizomes, gene transcripts encoding all nine enzymes were restricted to the protoderm of leaf primordia. The localization of biosynthetic gene transcripts was in contrast with the tissue-specific accumulation of protoberberine alkaloids. In roots, protoberberine alkaloids were restricted to mature endodermal cells upon the initiation of secondary growth and were distributed throughout the pith and cortex in rhizomes. Thus, the cell type-specific localization of protoberberine alkaloid biosynthesis and accumulation are temporally and spatially separated in T. flavum roots and rhizomes, respectively. Despite the close phylogeny between corresponding biosynthetic enzymes, distinct and different cell types are involved in the biosynthesis and accumulation of benzylisoquinoline alkaloids in T. flavum and P. somniferum. Our results suggest that the evolution of alkaloid metabolism involves not only the recruitment of new biosynthetic enzymes, but also the migration of established pathways between cell types.

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Purification and characterization of coclaurine N-methyltransferase from cultured Coptis japonica cells

Cited by 72 publications

References 17 publications

Cloning and Characterization of Naringenin 8-Prenyltransferase, a Flavonoid-Specific Prenyltransferase of Sophora flavescens

Cloning and Characterization of Naringenin 8-Prenyltransferase, a Flavonoid-Specific Prenyltransferase of Sophora flavescens

Benzylisoquinoline alkaloid biosynthesis in opium poppy

Cell Type–Specific Localization of Transcripts Encoding Nine Consecutive Enzymes Involved in Protoberberine Alkaloid Biosynthesis

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