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Information on EC 1.23.1.1 - (+)-pinoresinol reductase and Organism(s) Linum usitatissimum and UniProt Accession E6Y2X0
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1.23.1.1 (+)-pinoresinol reductaseIUBMB Comments
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that further reduces the product to the lignan (-)-secoisolariciresinol [EC 1.23.1.2, (+)-lariciresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) , Linum perenne (perennial flax) and Linum corymbulosum . The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol .
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Word Map
- 1.23.1.1
-
lignans
- secoisolariciresinol
- linum
- podophyllotoxin
- forsythia
-
+-pinoresinol
- usitatissimum
- intermedia
- album
-
dirigent
- matairesinol
- diglucoside
- flax
-
heartwood
- podophyllum
-
lignify
- cinnamoyl-coa
-
coniferyl
-
phenylcoumaran
-
cinnamyl-alcohol
- sesamin
-
cinnamyl
-
methylenedioxy
- cedar
The taxonomic range for the selected organisms is: Linum usitatissimum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pinoresinol-lariciresinol reductase, pinoresinol/lariciresinol reductase, pinoresinol reductase, luplr2, plr-lc1, (+)-pinoresinol/(+)-lariciresinol reductase, plr-la1, plr-lu2, (+)-pinoresinol-(+)-lariciresinol reductase, rr-pinoresinol-rr-lariciresinol reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
(+)-lariciresinol:NADP+ oxidoreductase
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that further reduces the product to the lignan (-)-secoisolariciresinol [EC 1.23.1.2, (+)-lariciresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6]. The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol [1].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
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-
-
?
additional information
?
-
(+)-pinoresinol is successively converted into (-+)-lariciresinol and further into (-)-secoisolariciresinol by bifunctional enzyme PrR2, cf. EC 1.23.1.2
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-
?
additional information
?
-
-
(+)-pinoresinol is successively converted into (-+)-lariciresinol and further into (-)-secoisolariciresinol by bifunctional enzyme PrR2, cf. EC 1.23.1.2
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
quantitative RT-PCR expression analysis of LuPLR1 and LuPLR2 expressions in leaves and seeds, steady-state level of LuPLR1 mRNA in leaf tissues. Spatiotemporal LuPLR2 gene expression pattern in relation to yatein biosynthesis. The LuPLR2 gene encoding the second PLR isoform is highly expressed in vegetative tissue with highest levels in young leaves and to a lesser extent in old leaves and stem
additional information
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quantitative RT-PCR expression analysis of LuPLR1 and LuPLR2 expressions in leaves and seeds, steady-state level of LuPLR1 mRNA in leaf tissues. Spatiotemporal LuPLR2 gene expression pattern in relation to yatein biosynthesis. The LuPLR2 gene encoding the second PLR isoform is highly expressed in vegetative tissue with highest levels in young leaves and to a lesser extent in old leaves and stem
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
identification of subcellular location of LuPLR2-derived lignan biosynthesis transgenic tobacco mesophyll cells that express LuPLR2-eGFP fusion proteins, LuPLR2 gene expression analysis
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additional information
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identification of subcellular location of LuPLR2-derived lignan biosynthesis transgenic tobacco mesophyll cells that express LuPLR2-eGFP fusion proteins, LuPLR2 gene expression analysis
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the biosynthetic pathway of lignans in 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
additional information
additional information
analysis of transcriptional regulation of the LuPLR2 gene from flax, overview. Spatiotemporal LuPLR2 gene expression pattern in relation to (-)-yatein biosynthesis
additional information
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analysis of transcriptional regulation of the LuPLR2 gene from flax, overview. Spatiotemporal LuPLR2 gene expression pattern in relation to (-)-yatein biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PILR2_LINUS
330
0
36499
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isozyme LuPLR2 overexpression in Linum usitatissimum plants causes yatein accumulation. The deletion of the region from -473 to -170, containing four putative-binding sites for the WRKY transcription factor involved in the response to wounding or elicitors, results in a complete loss of the response to both methyljasmonate treatment and wounding. A significant decrease in the LuPLR2 gene expression is caused by the deletion of the region from -826 to -473, which contains two putative two binding sites for the WRKY transcription factor, involved in the plant defense response, overview. The four regions, among known cis-motifs from plants, reveal the presence of two MYB-binding sites
additional information
-
isozyme LuPLR2 overexpression in Linum usitatissimum plants causes yatein accumulation. The deletion of the region from -473 to -170, containing four putative-binding sites for the WRKY transcription factor involved in the response to wounding or elicitors, results in a complete loss of the response to both methyljasmonate treatment and wounding. A significant decrease in the LuPLR2 gene expression is caused by the deletion of the region from -826 to -473, which contains two putative two binding sites for the WRKY transcription factor, involved in the plant defense response, overview. The four regions, among known cis-motifs from plants, reveal the presence of two MYB-binding sites
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 transcriptional regulation of the LuPLR2 gene
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
analysis of transcriptional regulation of the LuPLR2 gene from flax by a PCR walking strategy, overview
methyljasmonate triggers the expression of LuPLR2 leading to an over-accumulation of yatein, while salicylic acid fails to act strongly on the expression of this gene and yatein accumulation is not stimulated. LuPLR2 gene expression shows an increase in wounded plants, LuPLR2 gene expression is induced in wounded leaves compared to the control, cis-elements, responsible for gene expression in response to stress, are located in separate portions of the LuPLR2 promoter. LuPLR2 expression and yatein production are increased by methyl jasmonate and wounding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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), Linum usitatissimum
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), Linum usitatissimum
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Release 2023.1 (January 2023)
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