Prenylation of Flavonoids by Biotransformation of Yeast Expressing Plant Membrane-Bound Prenyltransferase SfN8DT-1

Sasaki, Kenji; Tsurumaru, Yusuke; Yazaki, Kazufumi

doi:10.1271/bbb.80729

Cited by 37 publications

(35 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Thus, the isolation of serial genes coding for prenyltransferases, which specifically recognize either group of flavonoid (flavanone, isoflavone, chalcone, or pterocarpan) as pronyl acceptor, has been achieved. Although the native substrate of SfiLDT may be different from isoliquiritigenin because prenylated isoliquiritigenin derivatives have not been identified in S. flavescens yet, production of various prenylated flavonoids became feasible by biotransformation using a yeast transformant expressing this prenyltransferase, as we previously showed with SfN8DT-1 (42). In application to plants, the isoflavone-specific prenyltransferase SfG6DT is expected to be a useful tool for metabolic engineering toward the molecular breeding of pathogen-resistant crops such as the pea, alfalfa, and licorice.…”

Section: S Fn 8d T -1 M Gs M Ll As F Pg As S It T G G S C Lr S K Q Yamentioning

confidence: 95%

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

Sasaki

Tsurumaru

Yamamoto

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Prenylated isoflavones are secondary metabolites that are mainly distributed in legume plants. They often possess divergent biological activities such as anti-bacterial, anti-fungal, and anti-oxidant activities and thus attract much attention in food, medicinal, and agricultural research fields. Prenyltransferase is the key enzyme in the biosynthesis of prenylated flavonoids by catalyzing a rate-limiting step, i.e. the coupling process of two major metabolic pathways, the isoprenoid pathway and shikimate/polyketide pathway. However, so far only two genes have been isolated as prenyltransferases involved in the biosynthesis of prenylated flavonoids, namely naringenin 8-dimethylallyltransferase from Sophora flavescens (SfN8DT-1) specific for some limited flavanones and glycinol 4-dimethylallyltransferase from Glycine max (G4DT), specific for pterocarpan substrate. We have in this study isolated two novel genes coding for membrane-bound flavonoid prenyltransferases from S. flavescens, an isoflavone-specific prenyltransferase (SfG6DT) responsible for the prenylation of the genistein at the 6-position and a chalcone-specific prenyltransferase designated as isoliquiritigenin dimethylallyltransferase (SfiLDT). These prenyltransferases were enzymatically characterized using a yeast expression system. Analysis on the substrate specificity of chimeric enzymes between SfN8DT-1 and SfG6DT suggested that the determinant region for the specificity of the flavonoids was the domain neighboring the fifth transmembrane ␣-helix of the prenyltransferases.

show abstract

Section: S Fn 8d T -1 M Gs M Ll As F Pg As S It T G G S C Lr S K Q Yamentioning

confidence: 95%

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

Sasaki

Tsurumaru

Yamamoto

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…A previous study had shown that the bioconversion from naringenin to 8DN by SfN8DT-1 ranged from 0.5% to 2% in the W303-1A-Dcoq2 yeast strain (for complete details of the genetic background, see Supplemental Table S1 and Supplemental Fig. S1D; Sasaki et al, 2009). We thus selected the DD104 strain for use in our hop prenyltransferase study.…”

Section: Yeast Strain Selection For Membrane-bound Aromatic Prenyltramentioning

confidence: 99%

A Heteromeric Membrane-Bound Prenyltransferase Complex from Hop Catalyzes Three Sequential Aromatic Prenylations in the Bitter Acid Pathway

et al. 2015

View full text Add to dashboard Cite

Bitter acids (a and b types) account for more than 30% of the fresh weight of hop (Humulus lupulus) glandular trichomes and are well known for their contribution to the bitter taste of beer. These multiprenylated chemicals also show diverse biological activities, some of which have potential benefits to human health. The bitter acid biosynthetic pathway has been investigated extensively, and the genes for the early steps of bitter acid synthesis have been cloned and functionally characterized. However, little is known about the enzyme(s) that catalyze three sequential prenylation steps in the b-bitter acid pathway. Here, we employed a yeast (Saccharomyces cerevisiae) system for the functional identification of aromatic prenyltransferase (PT) genes. Two PT genes (HlPT1L and HlPT2) obtained from a hop trichome-specific complementary DNA library were functionally characterized using this yeast system. Coexpression of codon-optimized PT1L and PT2 in yeast, together with upstream genes, led to the production of bitter acids, but no bitter acids were detected when either of the PT genes was expressed by itself. Stepwise mutation of the aspartate-rich motifs in PT1L and PT2 further revealed the prenylation sequence of these two enzymes in b-bitter acid biosynthesis: PT1L catalyzed only the first prenylation step, and PT2 catalyzed the two subsequent prenylation steps. A metabolon formed through interactions between PT1L and PT2 was demonstrated using a yeast two-hybrid system, reciprocal coimmunoprecipitation, and in vitro biochemical assays. These results provide direct evidence of the involvement of a functional metabolon of membrane-bound prenyltransferases in bitter acid biosynthesis in hop.

show abstract

“…Naringenin 8-dimethylallytransferase (SfN8DT-1) is the first flavonoid prenyltransferase identified from S. flavescens by Sasaki, Tsurumaru, and Yazaki (2009). Sasaki and his co-workers studied the prenylation of naringenin by biotransformation of yeast overexpressing SfN8DT-1.…”

Section: Biological Synthesismentioning

confidence: 99%

Prenylated flavonoids, promising nutraceuticals with impressive biological activities

Yang

Jiang

Yang

et al. 2015

Trends in Food Science & Technology

149

105

View full text Add to dashboard Cite

Prenylation of Flavonoids by Biotransformation of Yeast Expressing Plant Membrane-Bound Prenyltransferase SfN8DT-1

Cited by 37 publications

References 12 publications

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

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

A Heteromeric Membrane-Bound Prenyltransferase Complex from Hop Catalyzes Three Sequential Aromatic Prenylations in the Bitter Acid Pathway

Prenylated flavonoids, promising nutraceuticals with impressive biological activities

Contact Info

Product

Resources

About