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Information on EC 1.23.1.3 - (-)-pinoresinol reductase and Organism(s) Linum usitatissimum and UniProt Accession Q4R0H9
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1.23.1.3 (-)-pinoresinol reductaseIUBMB Comments
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (-)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) , Linum perenne (perennial flax) and Arabidopsis thaliana (thale cress) .
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Word Map
- 1.23.1.3
-
lignans
-
linum
- usitatissimum
- flax
- secoisolariciresinol
- diglucoside
- rnai
-
abscisic
-
promoter-reporter
-
flaxseed
-
cis-acting
- album
- forsythia
-
spatio-temporal
-
enantiospecific
-
hairy
- elicitors
-
rnai-mediated
-
chemopreventive
-
phytoestrogenic
-
phenylpropanoid
- intermedia
-
aerial
- podophyllotoxin
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
luplr1, pinoresinol lariciresinol reductase, plr-lu1, bifunctional pinoresinol-lariciresinol reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PLR-Lu1
additional information
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(-)-lariciresinol:NADP+ oxidoreductase
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (-)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].
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
(-)-lariciresinol + NADPH + H+
(+)-secoisolariciresinol + NADP+
-
-
-
-
?
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
-
-
-
-
?
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
-
-
-
?
additional information
?
-
(-)-pinoresinol is successively converted into (-)-lariciresinol and (+)-secoisolariciresinol by isozyme PrR1, cf. Ec 1.23.1.4
-
-
?
additional information
?
-
-
(-)-pinoresinol is successively converted into (-)-lariciresinol and (+)-secoisolariciresinol by isozyme PrR1, cf. Ec 1.23.1.4
-
-
?
additional information
?
-
-
(-)-pinoresinol is successively converted into (-)-lariciresinol and (+)-secoisolariciresinol by isozyme LuPLR1, cf. EC 1.23.1.4
-
-
?
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
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
-
-
-
?
additional information
?
-
(-)-pinoresinol is successively converted into (-)-lariciresinol and (+)-secoisolariciresinol by isozyme PrR1, cf. Ec 1.23.1.4
-
-
?
additional information
?
-
-
(-)-pinoresinol is successively converted into (-)-lariciresinol and (+)-secoisolariciresinol by isozyme PrR1, cf. Ec 1.23.1.4
-
-
?
additional information
?
-
-
(-)-pinoresinol is successively converted into (-)-lariciresinol and (+)-secoisolariciresinol by isozyme LuPLR1, cf. EC 1.23.1.4
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
cell layer-specific localization of secoisolariciresinol diglucoside (SDG) in flaxseed coats
the parenchymatous cell layer of the outer integument of flaxseed coats, the enzyme is strongly expressed in the seed coats of developing flaxseed, quantitative RT-PCR expression analysis or recombinant PLR1 promoter construct in transgenic flaxseed
additional information
spatiotemporal regulation of LuPLR1 gene expression in flaxseed, overview
additional information
LuPLR1 RT-PCR expression analysis in different organs, no expression of isozyme LuPLR1 in stems and leaves
additional information
-
LuPLR1 RT-PCR expression analysis in different organs, no expression of isozyme LuPLR1 in stems and leaves
additional information
no enzyme activity is detected in the inner integument and the embryo regardless of the developmental stage
additional information
-
no enzyme activity is detected in the inner integument and the embryo regardless of the developmental stage
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
malfunction
-
RNAi-generated plants exhibit LuPLR1 gene silencing and fail to accumulate secoisolariciresinol diglucoside (SDG). The accumulation of pinoresinol, the substrate of the PLR1 enzyme, in its diglucosylated form (PDG) is increased in transgenic seeds but does not compensate the overall loss of SDG. The monolignol flux is also deviated through the synthesis of 8-5'-linked neolignans dehydrodiconiferyl alcohol glucoside (DCG) and dihydro-dehydrodiconiferyl alcohol glucoside (DDCG)
metabolism
the enzyme is involved in the biosynthetic pathway of secoisolariciresinol diglucoside in flax Linum usitatissimum, overview. The correlation coefficient between LuPLR1 gene expression and lignan yatein accumulation is low
metabolism
the pinoresinol-lariciresinol reductase gene, LuPLR1, encoding bifunctional pinoresinol-lariciresinol reductase, is a key gene involved in secoisolariciresinol diglucoside (SDG) biosynthesis, proposed biosynthesis pathway of SDG oligomer, overview
physiological function
isozyme LuPLR1 catalyzes the biosynthesis of (+)-secoisolariciresinol ((+)-SECO) leading to (+)-secoisolariciresinol diglucoside in seeds
physiological function
the pinoresinol-lariciresinol reductase gene, LuPLR1, encoding bifunctional pinoresinol-lariciresinol reductase, is a key gene involved in secoisolariciresinol diglucoside (SDG) biosynthesis, responsible for the synthesis of the enantiomer (+)-secoisolariciresinol, spatiotemporal regulation of LuPLR1 gene expression in flaxseed, overview
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). PILR1_LINUS
312
0
35032
Swiss-Prot
other Location (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
RNAi-mediated pinoresinol lariciresinol reductase gene silencing, via Agrobacterium tumefaciens strain GV301 transformation, in Linum usitatissimum seed coat with consequences on lignans and neolignans accumulation, LuPLR1 transcript level is strongly reduced in the seeds ofPLR-RNAi plants, phenotype, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the promoter of one pinoresinol-lariciresinol reductase gene LuPLR1 is fused to a beta-glucuronidase (GUS) reporter gene, and the spatiotemporal regulation of LuPLR1 gene expression via this promoter in flaxseed is determined by histochemical and activity assays of GUS, recombinant expression of the promoter construct in transgenic flaxseed via transformation with Agrobacterium tumefaciens, quantitative RT-PCR expression analysis
gene PLR_Lu1, DNA and amino acid sequence determination and analysis, quantitative real-time RT-PCR enzyme expression analysis
-
the plasmid is transferred into the disarmed Agrobacter tumefaciens strain GV3101 by triparental mating with Escherichia coli strain HB101 and then introduced into Linum usitatissimum (cv. Barbara) transgenic plants
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of the PLR1 gene in the seed coat is down-regulated about 3fold when 0.01 mM fluridone is applied
-
the expression of the PLR1 gene in the seed coat is up-regulated about 3fold by 0.1 mM exogenous abscisic acid. There is a high mid-maturation expression of PLR1 gene between developmental stage 2 and stage
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 usitatissimum (Q4R0H9)
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
Hano, C.; Martin, I.; Fliniaux, O.; Legrand, B.; Gutierrez, L.; Arroo, R.R.; Mesnard, F.; Lamblin, F.; Laine, E.
Pinoresinol-lariciresinol reductase gene expression and secoisolariciresinol diglucoside accumulation in developing flax (Linum usitatissimum) seeds
Planta
224
1291-1301
2006
Linum usitatissimum
Renouard, S.; Corbin, C.; Lopez, T.; Montguillon, J.; Gutierrez, L.; Lamblin, F.; Laine, E.; Hano, C.
Abscisic acid regulates pinoresinol-lariciresinol reductase gene expression and secoisolariciresinol accumulation in developing flax (Linum usitatissimum L.) seeds
Planta
235
85-98
2012
Linum usitatissimum
Fang, J.; Ramsay, A.; Renouard, S.; Hano, C.; Lamblin, F.; Chabbert, B.; Mesnard, F.; Schneider, B.
Laser microdissection and spatiotemporal pinoresinol-lariciresinol reductase gene expression assign the cell layer-specific accumulation of secoisolariciresinol diglucoside in flaxseed coats
Front. Plant Sci.
7
1743
2016
Linum usitatissimum (Q4R0H9), Linum usitatissimum
Renouard, S.; Tribalatc, M.A.; Lamblin, F.; Mongelard, G.; Fliniaux, O.; Corbin, C.; Marosevic, D.; Pilard, S.; Demailly, H.; Gutierrez, L.; Hano, C.; Mesnard, F.; Laine, E.
RNAi-mediated pinoresinol lariciresinol reductase gene silencing in flax (Linum usitatissimum L.) seed coat consequences on lignans and neolignans accumulation
J. Plant Physiol.
171
1372-1377
2014
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 (Q4R0H9), Linum usitatissimum
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