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Enzyme Nomenclature
Information on EC 1.23.1.1 - (+)-pinoresinol reductase
Word Map on EC 1.23.1.1
- 1.23.1.1
-
lignans
- secoisolariciresinol
- linum
-
reductases
- podophyllotoxin
- forsythia
-
+-pinoresinol
- usitatissimum
-
phenylcoumaran
- intermedia
- flax
- album
-
heartwood
- matairesinol
- cinnamoyl-coa
- podophyllum
-
diglucoside
-
phytoestrogenic
- sesamin
-
dirigent
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.23.1.1
-
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RECOMMENDED NAME
GeneOntology No.
(+)-pinoresinol reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(+)-lariciresinol + NADP+ = (+)-pinoresinol + NADPH + H+
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
(+)-pinoresinol/(+)-lariciresinol reductase is a pivotal branchpoint enzyme in lignan biosynthesis
metabolism
the enzyme is involved in the enantiomeric control in lignan biosynthesis
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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+
efficient substrate
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
the enzyme abstracts the 4 pro-R hydrogen form NADPH (but not the 4 pro-S hydrogen)
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
primary substrate
-
-
?
(+/-)-pinoresinol + NADPH + H+
(+/-)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-pinoresinol + NADPH + H+
(+/-)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
additional information
?
-
-
the activity toward (+/-)-lariciresinol is 35times lower than that of pinoresinol
-
-
-
additional information
?
-
the activity toward (+/-)-lariciresinol is 35times lower than that of pinoresinol
-
-
-
additional information
?
-
-
(-)-pinoresinol does not serve as substrate
-
-
-
additional information
?
-
-
sesamin is not reduced by the enzyme
-
-
-
additional information
?
-
the protein shows preference for (+)-pinoresinol (R,R configuration at C-atoms 8,8’) in the first reaction step, but preference for (-)-lariciresinol (S,S configuration at C-atoms 8,8’) in the second reaction step
-
-
-
additional information
?
-
-
the protein shows preference for (+)-pinoresinol (R,R configuration at C-atoms 8,8’) in the first reaction step, but preference for (-)-lariciresinol (S,S configuration at C-atoms 8,8’) in the second reaction step
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
activity is 15fold higher with NADPH than that in the presence of NADH, suggesting that NADPH is a preferred electron donor
NADPH
-
activity is 7fold higher with NADPH than that in the presence of NADH, suggesting that NADPH is a preferred electron donor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32
-
toward (+/-)-pinoresinol in the presence of NADPH, at pH 7.0 and 30°C
46
-
toward (+/-)-syringaresinol in the presence of NADPH, at pH 7.0 and 30°C
61
-
toward (+/-)-syringaresinol in the presence of NADPH, at pH 7.0 and 30°C
82.18
-
using (+)-pinoresinol and [4R]-NADPH as substrates, at pH 8.0 and 30°C
additional information
additional information
-
1 micromol/min/mg specific activity toward (+/-)-lariciresinol in the presence of NADPH, at pH 7.0 and 30°C
additional information
-
1 micromol/mg/min specific activity towards (+/-)-lariciresinol in the presence of NADPH, at pH 7.0 and 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer or dimer
-
x * 35000-36000, SDS-PAGE; x * 39400, calculated from amino acid sequence
monomer
-
1 * 36000, recombinant enzyme, SDS-PAGE; 1 * 36837, calculated from amino acid sequence
monomer
-
1 * 36000, recombinant enzyme, SDS-PAGE; 1 * 36837, calculated from amino acid sequence
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, Affinity Blue Gel filtration, phenyl Sepharose column chromatography, hydroxyapatite column chromatography, 2’,5’ ADP-Sepharose column chromatography, Affinity-Yellow gel filtration, and Superose 12 gel filtration
-
ammonium sulfate precipitation and Affi-Gel Blue Gel column chromatography
-
nickel affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Triticum aestivum cultivars Bobwhite, Madison, and Fielder
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LINKS TO OTHER DATABASES (specific for EC-Number 1.23.1.1)
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