Information on EC 1.23.1.1 - (+)-pinoresinol reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
1.23.1.1
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RECOMMENDED NAME
GeneOntology No.
(+)-pinoresinol reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-lariciresinol + NADP+ = (+)-pinoresinol + NADPH + H+
show the reaction diagram
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
matairesinol biosynthesis
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-
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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 hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
show the reaction diagram
medioresinol + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
syringaresinol + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
(+)-pinoresinol
at pH 7.5 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8
(+)-pinoresinol
Arabidopsis thaliana
Q9FVQ6
at pH 7.5 and 30°C
37822
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000083
-
crude extract, at pH 7.4 and 30°C
0.255
-
after 3060fold purification, at pH 7.4 and 30°C
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
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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-
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
isoelectric focusing
7.1
-
calculated from amino acid sequence
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
gel filtration
36000
-
1 * 36000, recombinant enzyme, SDS-PAGE
36400
x * 36400, calculated from amino acid sequence
36837
-
1 * 36837, calculated from amino acid sequence
39400
-
x * 39400, calculated from amino acid sequence
59000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 36400, calculated from amino acid sequence
monomer
monomer or dimer
-
x * 35000-36000, SDS-PAGE; x * 39400, 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
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ammonium sulfate precipitation and Affi-Gel Blue Gel column chromatography
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His-Bind resin affinity column chromatography
metal chelate chromatography
Ni-NTA column chromatography
nickel affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in BL21 (DE3)-RIL cells
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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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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)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)