Information on EC 1.23.1.3 - (-)-pinoresinol reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.23.1.3
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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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
matairesinol biosynthesis
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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 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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the enantiomeric control in lignan biosynthesis; the enzyme is involved in the enantiomeric control in lignan biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-lariciresinol + NADPH + H+
(+)-secoisolariciresinol + NADP+
show the reaction diagram
(-)-pinoresinol + NADPH + H+
(-)-lariciresinol + NADP+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0073 - 0.0126
(-)-pinoresinol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.17 - 19
(-)-pinoresinol
20027
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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not expressed in leaf and stem
Manually annotated by BRENDA team
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, using 20% (w/v) polyethylene glycol 8000, 0.1 M MES, pH 6.2, 0.1 M NaCl, and 0.1 M calcium acetate
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-Bind resin affinity column chromatography; His-Bind resin affinity column chromatography
Ni-NTA column chromatography
POROS 20 HQ column chromatography and ADP-agarose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834-DE3 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 strain HB101
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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
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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
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