Pinoresinol–lariciresinol reductases with different stereospecificity from Linum album and Linum usitatissimum

Heimendahl, Cosima B. I. von; Schäfer, Katrin M.; Eklund, Patrik; Sjöholm, Rainer; Schmidt, Thomas J.; Fuss, Elisabeth

doi:10.1016/j.phytochem.2005.04.026

Cited by 61 publications

(61 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This is in line with the selectivity of substrate enantiomers of PLRs from other plants. Forsythia intermedia PLR (PLR-Fi1) (21), Thuja plicata PLR2 (PLR-Tp2) (16), and Linum album PLR1 (PLR-La1) (22) all catalyzed the selective reduction of (ϩ)-pinoresinol to (ϩ)-lariciresinol and (Ϫ)-secoisolariciresinol, whereas T. plicata PLR1 (PLR-Tp1) (16), and Linum usitatissimum PLR1 (PLR-Lu1) (22) (Fig. 5).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Arabidopsis thaliana Pinoresinol Reductase, a New Type of Enzyme Involved in Lignan Biosynthesis

Nakatsubo

Mizutani

Suzuki

et al. 2008

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

A lignan, lariciresinol, was isolated from Arabidopsis thaliana, the most widely used model plant in plant bioscience sectors, for the first time. In the A. thaliana genome database, there are two genes (At1g32100 and At4g13660) that are annotated as pinoresinol/lariciresinol reductase (PLR). The recombinant AtPLRs showed strict substrate preference toward pinoresinol but only weak or no activity toward lariciresinol, which is in sharp contrast to conventional PLRs of other plants that can reduce both pinoresinol and lariciresinol efficiently to lariciresinol and secoisolariciresinol, respectively. Therefore, we renamed AtPLRs as A. thaliana pinoresinol reductases (AtPrRs).

show abstract

Section: Discussionmentioning

confidence: 99%

Characterization of Arabidopsis thaliana Pinoresinol Reductase, a New Type of Enzyme Involved in Lignan Biosynthesis

Nakatsubo

Mizutani

Suzuki

et al. 2008

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

show abstract

“…In the last few years, a large number of these reductases (so-called IFR "homologues") have been identiWed in various plant species, woody and non-woody angiosperms and gymnosperms (Davin and Lewis 2003). Lewis et al (2001) andvon Heimendahl et al (2005) have cloned and published Xax PLR encoding cDNAs. Previous experiments have led us to clone a number of Xax cDNAs involved in the regulation of phenylpropanoid pathway, amongst which the LuPLR and LuPCBER (Attoumbre et al 2006; AY837829) genes involved in lignan and neolignan metabolism.…”

Section: Introductionmentioning

confidence: 99%

Pinoresinol–lariciresinol reductase gene expression and secoisolariciresinol diglucoside accumulation in developing flax (Linum usitatissimum) seeds

Hano

Martín

Fliniaux

et al. 2006

Planta

111

View full text Add to dashboard Cite

The transcription activity of the pinoresinol-lariciresinol reductase (PLR) gene of Linum usitatissimum (so-called LuPLR), a key gene in lignan synthesis, was studied by RT-PCR and promoter-reporter transgenesis. The promoter was found to drive transcription of a GUSint reporter gene in the seed coats during the flax seed development. This fitted well with the tissue localization monitored by semi-quantitative RT-PCR of LuPLR expression. Accumulation of the main flax lignan secoisolariciresinol diglucoside was coherent with LuPLR expression during seed development. This three-way approach demonstrated that the LuPLR gene is expressed in the seed coat of flax seeds, and that the synthesis of PLR enzyme occurs where flax main lignan is found stored in mature seeds, confirming its involvement in SDG synthesis.

show abstract

“…The enzyme PLR has been identified in Forsythia intermedia (15), Thuja plicata (18), Linum perenne (20), L. album, and L. usitatissimum (19). We cloned plr cDNA from P. pleianthum Hance.…”

Section: Discussionmentioning

confidence: 99%

“…All of the lignan reductases contain a conserved NADPH-binding domain, GxxGxxG, in a region close to the N terminus, and this NADPH-binding domain was also present in the deduced amino sequence of PLR-PpH. Although pinoresinol stereospecificity was initially reported to be determined by Leu 164 , Phe 272 , and Gly 268 (24), these residues were soon found not to be sufficient (19). Thus, the existence of Gly 268 and another aromatic amino acid, Tyr 272 , instead of Phe in the PLR-PpH sequence is not sufficient to explain the (ϩ)-pinoresinol substrate stereospecificity and suggests that other residues are also involved.…”

Section: Discussionmentioning

confidence: 99%

“…The primer sequences are listed in Table S1 in the supplemental material. Based on a multiple-sequence alignment of PLR-Fi1 (GenBank accession number U81158) (15), PLRTp1 (AF242503) (18), PLR-Tp2 (AF242504) (18), PLR-La1 (AJ849358) (19), and PLR-Lu1 (AJ849359) (19), the degenerate primers PLRFOR1, PLRFOR2, and PLRREV2 were designed to amplify the conserved part of plr. RT-PCR was performed using a OneStep RT-PCR kit with PLRFOR1 and oligo(dT), and the PCR product was further amplified using PLRFOR2 and PLRREV2.…”

Section: Chemicalsmentioning

confidence: 99%

See 1 more Smart Citation

Bioconversion of Pinoresinol into Matairesinol by Use of Recombinant Escherichia coli

Kuo

Wei

et al. 2014

Appl Environ Microbiol

View full text Add to dashboard Cite

Lignans, a class of dimeric phenylpropanoid derivative found in plants, such as whole grains and sesame and flax seeds, have anticancer activity and can act as phytoestrogens. The lignans secoisolariciresinol and matairesinol can be converted in the mammalian proximal colon into enterolactone and enterodiol, respectively, which reduce the risk of breast and colon cancer. To establish an efficient bioconversion system to generate matairesinol from pinoresinol, the genes encoding pinoresinol-lariciresinol reductase (PLR) and secoisolariciresinol dehydrogenase (SDH) were cloned from Podophyllum pleianthum Hance, an endangered herb in Taiwan, and the recombinant proteins, rPLR and rSDH, were expressed in Escherichia coli and purified. The two genes, termed plr-PpH and sdh-PpH, were also linked to form two bifunctional fusion genes, plr-sdh and sdh-plr, which were also expressed in E. coli and purified. Bioconversion in vitro at 22°C for 60 min showed that the conversion efficiency of fusion protein PLR-SDH was higher than that of the mixture of rPLR and rSDH. The percent conversion of (؉)-pinoresinol to matairesinol was 49.8% using PLR-SDH and only 17.7% using a mixture of rPLR and rSDH. However, conversion of (؉)-pinoresinol by fusion protein SDH-PLR stopped at the intermediate product, secoisolariciresinol. In vivo, (؉)-pinoresinol was completely converted to matairesinol by living recombinant E. coli expressing PLR-SDH without addition of cofactors.

show abstract

Pinoresinol–lariciresinol reductases with different stereospecificity from Linum album and Linum usitatissimum

Cited by 61 publications

References 22 publications

Characterization of Arabidopsis thaliana Pinoresinol Reductase, a New Type of Enzyme Involved in Lignan Biosynthesis

Characterization of Arabidopsis thaliana Pinoresinol Reductase, a New Type of Enzyme Involved in Lignan Biosynthesis

Pinoresinol–lariciresinol reductase gene expression and secoisolariciresinol diglucoside accumulation in developing flax (Linum usitatissimum) seeds

Bioconversion of Pinoresinol into Matairesinol by Use of Recombinant Escherichia coli

Contact Info

Product

Resources

About