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Synonyms
(+)-lariciresinol reductase, (+)-pinoresinol-(+)-lariciresinol reductase, (+)-pinoresinol/(+)-lariciresinol reductase, bi-functional pinoresinol/lariciresinol reductase, bifunctional pinoresinol-lariciresinol reductase 2, LuPLR2, More, pinoresinol reductase, pinoresinol reductase 2, pinoresinol-lariciresinol reductase,
more
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(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
(+)-lariciresinol + NADPH + H+
secoisolariciresinol + NADP+
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
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-
-
?
medioresinol + NADPH + H+
? + NADP+
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-
-
-
?
syringaresinol + NADPH + H+
? + NADP+
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-
-
?
additional information
?
-
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
the enzyme abstracts the 4 pro-R hydrogen form NADPH (but not the 4 pro-S hydrogen)
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-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
?
(+)-lariciresinol + NADPH + H+
(-)-secoisolariciresinol + NADP+
-
-
-
-
?
(+)-lariciresinol + NADPH + H+
secoisolariciresinol + NADP+
-
-
-
-
?
(+)-lariciresinol + NADPH + H+
secoisolariciresinol + NADP+
-
-
-
-
?
(+)-lariciresinol + NADPH + H+
secoisolariciresinol + NADP+
-
-
-
-
?
additional information
?
-
(+)-pinoresinol is successively converted into (-+)-lariciresinol and further into (-)-secoisolariciresinol by bifunctional enzyme PrR2, cf. EC 1.23.1.1. The pinoresinol reductase shows only weak activity toward lariciresinol
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-
?
additional information
?
-
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(-)-pinoresinol does not serve as substrate
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?
additional information
?
-
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sesamin is not reduced by the enzyme
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-
?
additional information
?
-
(+)-pinoresinol is successively converted into (-+)-lariciresinol and further into (-)-secoisolariciresinol by bifunctional enzyme PrR2, cf. EC 1.23.1.1
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-
?
additional information
?
-
(-+)-pinoresinol is successively converted into (-+)-lariciresinol and (-+)-secoisolariciresinol by enzyme PinZ
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-
?
additional information
?
-
-
no activity with (-)-lariciresinol
-
-
?
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additional information
analysis of transcriptional regulation of the LuPLR2 gene from flax, overview. Spatiotemporal LuPLR2 gene expression pattern in relation to yatein biosynthesis
metabolism
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(+)-pinoresinol/(+)-lariciresinol reductase is a pivotal branchpoint enzyme in lignan biosynthesis
metabolism
the enzyme participates in (-)-hinokinin biosynthesis in Linum corymbulosum by the first of the two hypothetical pathways via (-)-secoisolariciresinol
metabolism
pinoresinol is successively converted into lariciresinol and secoisolariciresinol by PrR. Secoisolariciresinol is glycosylated to secoisolariciresinol diglucoside (SDG). PLR has enantiomeric control on the lignan biosynthetic pathway
metabolism
the enzyme is involved in the biosynthetic pathway of lignans in flax Linum usitatissimum, overview
physiological function
LuPLR2 is involved in the early steps of (-)-secoisolariciresinol ((-)-SECO) biosynthesis and derived lignans (yatein, hinokinin, bursehernin, thujaplicatin, and matairesinol dimethyl ether) accumulated mainly in leaves. In vivo involvement of the LuPLR2 gene in the biosynthesis of (-)-yatein accumulated in flax leaves. The enzyme expression is correlated to yatein, a lignan, accumulation in plant leaves. Lignans are probably involved in plant defense mechanisms and given the presence of several cis-regulatory elements potentially involved in the plant defense response revealed by the in silico analysis of LuPLR2, presence of two MYB-binding sites in LuPLR2
physiological function
pinoresinol reductase catalyzes the conversion of the lignan pinoresinol to lariciresinol in Arabidopsis thaliana, where it is encoded by two genes, PrR1 and PrR2, that appear to act redundantly. The isozyme PrR2 is responsible for the synthesis of the enantiomer (-)-secoisolariciresinol
physiological function
recombinant expression of gene pinZ in Arabidopsis thaliana causes dynamic metabolic changes in stems, but not in roots and leaves. Expression of pinZ influenced the metabolisms of lignan and glucosinolates but not so much of neolignans such as guaiacylglycerol-8-O-4'-feruloyl ethers
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expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli Nova Blue cells
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expressed in Escherichia coli Nova-Blue cells
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gene pinZ, recombinant expression in Arabidopsis thaliana under the control of the cauliflower mosaic virus 35S promoter, pinZ expression causes dynamic metabolic changes in stems, but not in roots and leaves. Accumulation of the glucoside of secoisolariciresinol appears to be elevated in the transgenic plant. Expression of pinZ influenced the metabolisms of lignan and glucosinolates but not so much of neolignans such as guaiacylglycerol-8-O-4'-feruloyl ethers, recombinant enzyme tissue expression pattern in plant seedlings
gene PLR2, recombinant expression of N-terminal and C-terminal fusions of LuPLR2 with EGFP or GUS in transgenic tobacco mesophyll cells, and LuPLR2 overexpression in transgenic flax plants, via transformation by Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR expression analysis of LuPLR1 and LuPLR2 expressions in leaves and seeds, subcloning in Escherichia coli strain HB101. cis-Elements, responsible for gene expression in response to stress, are located in separate portions of the LuPLR2 promoter, presence of two MYB-binding sites. Quantitative RT-PCR expression analysis of LuPLR2 in transgenic seedlings, analysis of the transcriptional regulation of the LuPLR2 gene
gene PrP2, gene co-expression networks for Arabidopsis thaliana PrR1 and PrR2, overview. PrR2 expression clusters with a different set of genes, not involved in secondary cell wall biosynthesis
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Vassao, D.; Kim, S.; Milhollan, J.; Eichinger, D.; Davin, L.; Lewis, N.
A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeug
Arch. Biochem. Biophys.
465
209-218
2007
Forsythia x intermedia
brenda
Chu, A.; Dinkova, A.; Davin, L.B.; Bedgar, D.L.; Lewis, N.G.
Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia
J. Biol. Chem.
268
27026-27033
1993
Forsythia x intermedia
brenda
Fujita, M.; Gang, D.R.; Davin, L.B.; Lewis, N.G.
Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions
J. Biol. Chem.
274
618-627
1999
Thuja plicata
brenda
Xie, L.H.; Akao, T.; Hamasaki, K.; Deyama, T.; Hattori, M.
Biotransformation of pinoresinol diglucoside to mammalian lignans by human intestinal microflora, and isolation of Enterococcus faecalis strain PDG-1 responsible for the transformation of (+)-pinoresinol to (+)-lariciresinol
Chem. Pharm. Bull.
51
508-515
2003
Enterococcus faecalis, Enterococcus faecalis PDG-1
brenda
Dinkova-Kostova, A.T.; Gang, D.R.; Davin, L.B.; Bedgar, D.L.; Chu, A.; Lewis, N.G.
(+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase
J. Biol. Chem.
271
29473-29482
1996
Forsythia x intermedia
brenda
Katayama, T.; Davin, L.B.; Lewis, N.G.
An extraordinary accumulation of (-)-pinoresinol in cell-free extracts of Forsythia intermedia: evidence for enantiospecific reduction of (+)-pinoresinol
Phytochemistry
31
3875-3881
1992
Forsythia x intermedia
brenda
von Heimendahl, C.B.; Schaefer, K.M.; Eklund, P.; Sjoeholm, R.; Schmidt, T.J.; Fuss, E.
Pinoresinol-lariciresinol reductases with different stereospecificity from Linum album and Linum usitatissimum
Phytochemistry
66
1254-1263
2005
Linum album (Q4R0I0)
brenda
Bayindir, U.; Alfermann, A.W.; Fuss, E.
Hinokinin biosynthesis in Linum corymbulosum Reichenb.
Plant J.
55
810-820
2008
Linum corymbulosum (B5KRH5)
brenda
Hemmati, S.; von Heimendahl, C.B.; Klaes, M.; Alfermann, A.W.; Schmidt, T.J.; Fuss, E.
Pinoresinol-lariciresinol reductases with opposite enantiospecificity determine the enantiomeric composition of lignans in the different organs of Linum usitatissimum L.
Planta Med.
76
928-934
2010
Linum usitatissimum (E6Y2X0)
brenda
Tamura, M.; Tsuji, Y.; Kusunose, T.; Okazawa, A.; Kamimura, N.; Mori, T.; Nakabayashi, R.; Hishiyama, S.; Fukuhara, Y.; Hara, H.; Sato-Izawa, K.; Muranaka, T.; Saito, K.; Katayama, Y.; Fukuda, M.; Masai, E.; Kajita, S.
Successful expression of a novel bacterial gene for pinoresinol reductase and its effect on lignan biosynthesis in transgenic Arabidopsis thaliana
Appl. Microbiol. Biotechnol.
98
8165-8177
2014
Sphingobium sp. SYK-6 (G2IMF2)
brenda
Zhao, Q.; Zeng, Y.; Yin, Y.; Pu, Y.; Jackson, L.A.; Engle, N.L.; Martin, M.Z.; Tschaplinski, T.J.; Ding, S.Y.; Ragauskas, A.J.; Dixon, R.A.
Pinoresinol reductase 1 impacts lignin distribution during secondary cell wall biosynthesis in Arabidopsis
Phytochemistry
112
170-178
2015
Arabidopsis thaliana (Q9SVP6)
brenda
Corbin, C.; Drouet, S.; Mateljak, I.; Markulin, L.; Decourtil, C.; Renouard, S.; Lopez, T.; Doussot, J.; Lamblin, F.; Auguin, D.; Laine, E.; Fuss, E.; Hano, C.
Functional characterization of the pinoresinol-lariciresinol reductase-2 gene reveals its roles in yatein biosynthesis and flax defense response
Planta
246
405-420
2017
Linum usitatissimum (E6Y2X0)
brenda