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Information on EC 1.23.1.1 - (+)-pinoresinol reductase and Organism(s) Linum perenne and UniProt Accession A3R052

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EC Tree
     1 Oxidoreductases
         1.23 Reducing C-O-C group as acceptor
             1.23.1 With NADH or NADPH as donor
                1.23.1.1 (+)-pinoresinol reductase
IUBMB Comments
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) , Linum perenne (perennial flax) and Linum corymbulosum . The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol .
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Linum perenne
UNIPROT: A3R052
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Word Map
The taxonomic range for the selected organisms is: Linum perenne
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pinoresinol-lariciresinol reductase, pinoresinol/lariciresinol reductase, pinoresinol reductase, luplr2, plr-lc1, plr-la1, plr-lu2, (+)-pinoresinol/(+)-lariciresinol reductase, (+)-pinoresinol-(+)-lariciresinol reductase, rr-pinoresinol-rr-lariciresinol reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pinoresinol-lariciresinol reductase
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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].
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
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additional information
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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), Linum perenne
Manually annotated by BRENDA team