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Information on EC 1.23.1.3 - (-)-pinoresinol reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SVP6

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EC Tree
     1 Oxidoreductases
         1.23 Reducing C-O-C group as acceptor
             1.23.1 With NADH or NADPH as donor
                1.23.1.3 (-)-pinoresinol reductase
IUBMB 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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Arabidopsis thaliana
UNIPROT: Q9SVP6
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
luplr1, pinoresinol lariciresinol reductase, plr-lu1, bifunctional pinoresinol-lariciresinol reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bi-functional pinoresinol/lariciresinol reductase
-
pinoresinol reductase
-
pinoresinol reductase 1
-
additional information
cf. EC 1.23.1.4
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
show the reaction diagram
-
-
-
?
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0126
(-)-pinoresinol
at pH 7.5 and 30°C
0.0073
(-)-pinoresinol
at pH 7.5 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.17
(-)-pinoresinol
at pH 7.5 and 30°C
19
(-)-pinoresinol
at pH 7.5 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
transcript levels in root are higher than those in stem
Manually annotated by BRENDA team
transcript levels in root are higher than those in stem
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the enantiomeric control in lignan biosynthesis
malfunction
the loss-of-function mutant of PrR1 shows, in addition to elevated levels of pinoresinol, significantly decreased lignin content and a slightly altered lignin structure with lower abundance of cinnamyl alcohol end groups. Stimulated Raman scattering (SRS) microscopy analysis indicates that the lignin content of the prr1-1 loss-of-function mutant is similar to that of wild-type plants in xylem cells, which exhibit a normal phenotype, but is reduced in the fiber cells. The concentration of the lignan, pinoresinol, is 4.8fold higher in the loss-of-function prr1 mutant than in control plants. Impact of loss of function of PrR1 on the cellular distribution of lignin. The PrR1 isozyme mutation alters the expression level of diverse genes, overview
metabolism
physiological function
pinoresinol reductase (PrR) 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. Association of the lignan biosynthetic enzyme encoded by PrR1 with secondary cell wall biosynthesis in fiber cells. PrR1 is regulated by the secondary cell wall transcription factors SND1 and MYB46. PrR1 plays a role in lignan biosynthesis in aerial tissue
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PILR2_ARATH
317
0
35415
Swiss-Prot
other Location (Reliability: 4)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Bind resin affinity column chromatography
His-Bind resin affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 (DE3) cells
gene PrR1, PrR1 is co-expressed with many characterized genes involved in secondary cell wall biosynthesis, gene co-expression networks for Arabidopsis thaliana PrR1 and PrR2, overview. PrR1 is regulated by the secondary cell wall transcription factors SND1 and MYB46
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakatsubo, T.; Mizutani, M.; Suzuki, S.; Hattori, T.; Umezawa, T.
Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis
J. Biol. Chem.
283
15550-15557
2008
Arabidopsis thaliana (Q9FVQ6), Arabidopsis thaliana (Q9SVP6)
Manually annotated by BRENDA team
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 (Q9FVQ6), Arabidopsis thaliana
Manually annotated by BRENDA team