Flavonoid 3′-O-methyltransferase from rice: cDNA cloning, characterization and functional expression

Kim, Bong-Gyu; Lee, Youngshim; Hur, Hor‐Gil; Lim, Yoongho; Ahn, Joong‐Hoon

doi:10.1016/j.phytochem.2005.11.022

Cited by 118 publications

(97 citation statements)

References 15 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). …”

Section: Resultssupporting

confidence: 76%

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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Section: Resultssupporting

confidence: 76%

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

et al. 2008

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“…1). However, a substrate specificity of some plant class I methyltransferases also for flavonoids was reported in a recent study (Ibdah et al, 2003;Kim et al, 2006). Moreover, rat COMT, another class I methyltransferase, is known to accept flavonoids as substrates (Zhu et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Over‐expression of an S‐adenosylmethionine‐dependent methyltransferase leads to an extended lifespan of Podospora anserina without impairments in vital functions

Kunstmann

Osiewacz

2008

Aging Cell

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SummaryPaMTH1, a putative methyltransferase previously described to increase in abundance in total protein extracts during aging of Podospora anserina is demonstrated to accumulate in the mitochondrial cell fraction of senescent cultures. The protein is localized in the mitochondrial matrix and displays a methyltransferase activity utilizing flavonoids as substrates. Constitutive over-expression of PaMth1 in P. anserina results in a reduced carbonylation of proteins and an extended lifespan without impairing vital functions suggesting a protecting role of PaMTH1 against oxidative stress.

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“…The resulting fusion protein was induced with IPTG (isopropyl-β-D-thiogalactoside) in E. coli as described (11). The recombinant OsFNS I-1 fusion protein was purified with a glutathione S-transferase affinity column (Amersham Biotech, USA) according to the manufacturer's instruction.…”

Section: Methodsmentioning

confidence: 99%

“…Purified OsFNS I-1 was incubated with 1 mM ascorbate, 50 μM FeSO4, 100 mg/ml catalase, 160 μM oxoglutarate, and 60 μM of S or R-naringenin in 500 μl of 10 μM Tris/HCl buffer (pH 8.0) for 3 hr at 37 o C. The reaction product was analyzed using HPLC as described by (11).…”

Section: Enzyme Assay and Reaction Product Analysismentioning

confidence: 99%

Characterization of flavone synthase I from rice

Lee¹,

Kim²,

Kim³

et al. 2008

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Flavonoid 3′-O-methyltransferase from rice: cDNA cloning, characterization and functional expression

Cited by 118 publications

References 15 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

Over‐expression of an S‐adenosylmethionine‐dependent methyltransferase leads to an extended lifespan of Podospora anserina without impairments in vital functions

Characterization of flavone synthase I from rice

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