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Information on EC 1.23.1.4 - (-)-lariciresinol reductase and Organism(s) Linum perenne and UniProt Accession A3R052

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IUBMB Comments
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (-)-pinoresinol [EC 1.23.1.3, (-)-pinoresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) and Linum corymbulosum .
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This record set is specific for:
Linum perenne
UNIPROT: A3R052
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The taxonomic range for the selected organisms is: Linum perenne
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
()-pinoresinol-()-lariciresinol reductase, bi-functional pinoresinol/lariciresinol reductase, bifunctional pinoresinol-lariciresinol reductase, bifunctional pinoresinol-lariciresinol reductase 1, LuPLR1, More, pinoresinol lariciresinol reductase, pinoresinol reductase, pinoresinol reductase 1, pinoresinol-lariciresinol reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pinoresinol-lariciresinol reductase
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SYSTEMATIC NAME
IUBMB Comments
(+)-secoisolariciresinol:NADPH+ oxidoreductase
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (-)-pinoresinol [EC 1.23.1.3, (-)-pinoresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1] and Linum corymbulosum [2].
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
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-
-
?
additional information
?
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the biosynthesis of justicidin B
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PILR1_LINPE
314
0
35226
Swiss-Prot
other Location (Reliability: 4)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
metal chelate chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in BL21 (DE3)-RIL cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hemmati, S.; Schmidt, T.J.; Fuss, E.
(+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B
FEBS Lett.
581
603-610
2007
Linum perenne (A3R052)
Manually annotated by BRENDA team