Information on EC 1.23.1.2 - (+)-lariciresinol reductase

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

EC NUMBER
COMMENTARY hide
1.23.1.2
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RECOMMENDED NAME
GeneOntology No.
(+)-lariciresinol reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-secoisolariciresinol + NADP+ = (+)-lariciresinol + 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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SYSTEMATIC NAME
IUBMB Comments
(–)-secoisolariciresinol:NADP+ oxidoreductase
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (+)-pinoresinol [EC 1.23.1.1, (+)-pinoresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
(+)-lariciresinol + NADPH + H+
secoisolariciresinol + NADP+
show the reaction diagram
medioresinol + NADPH + H+
? + NADP+
show the reaction diagram
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-
-
-
?
syringaresinol + NADPH + H+
? + NADP+
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000083
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crude extract, at pH 7.4 and 30°C
0.255
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after 3060fold purification, at pH 7.4 and 30°C
131.4
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using (+)-secoisolariciresinol and [4R]-NADPH as substrates, at pH 8.0 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
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isoelectric focusing
7.1
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calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest expression
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36400
x * 36400, calculated from amino acid sequence
39400
-
x * 39400, calculated from amino acid sequence
59000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 36400, calculated from amino acid sequence
monomer or dimer
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x * 35000-36000, SDS-PAGE; x * 39400, calculated from amino acid sequence
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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Ni-NTA column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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