Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
(+/-)-pinoresinol + NADPH + H+
(+/-)-lariciresinol + NADP+
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
medioresinol + NADPH + H+
? + NADP+
-
-
-
-
?
syringaresinol + NADPH + H+
? + NADP+
-
-
-
-
?
additional information
?
-
(+)-pinoresinol + NADPH + H+

(+)-lariciresinol + NADP+
efficient substrate
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
the enzyme abstracts the 4 pro-R hydrogen form NADPH (but not the 4 pro-S hydrogen)
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
primary substrate
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
?
(+)-pinoresinol + NADPH + H+
(+)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-pinoresinol + NADPH + H+

(+/-)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-pinoresinol + NADPH + H+
(+/-)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-pinoresinol + NADPH + H+
(+/-)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-pinoresinol + NADPH + H+
(+/-)-lariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+

5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
(+/-)-syringaresinol + NADPH + H+
5,5'-dimethoxylariciresinol + NADP+
-
-
-
-
?
additional information

?
-
-
the activity toward (+/-)-lariciresinol is 35times lower than that of pinoresinol
-
-
-
additional information
?
-
the activity toward (+/-)-lariciresinol is 35times lower than that of pinoresinol
-
-
-
additional information
?
-
-
(-)-pinoresinol does not serve as substrate
-
-
-
additional information
?
-
-
sesamin is not reduced by the enzyme
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
additional information
?
-
-
negligible activity with (+/-)-lariciresinol compared to (+/-)-pinoresinol
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Vassao, D.; Kim, S.; Milhollan, J.; Eichinger, D.; Davin, L.; Lewis, N.
A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeug
Arch. Biochem. Biophys.
465
209-218
2007
Forsythia x intermedia
brenda
Chu, A.; Dinkova, A.; Davin, L.B.; Bedgar, D.L.; Lewis, N.G.
Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia
J. Biol. Chem.
268
27026-27033
1993
Forsythia x intermedia
brenda
Fujita, M.; Gang, D.R.; Davin, L.B.; Lewis, N.G.
Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions
J. Biol. Chem.
274
618-627
1999
Thuja plicata
brenda
Xie, L.H.; Akao, T.; Hamasaki, K.; Deyama, T.; Hattori, M.
Biotransformation of pinoresinol diglucoside to mammalian lignans by human intestinal microflora, and isolation of Enterococcus faecalis strain PDG-1 responsible for the transformation of (+)-pinoresinol to (+)-lariciresinol
Chem. Pharm. Bull.
51
508-515
2003
Enterococcus faecalis, Enterococcus faecalis PDG-1
brenda
Fukuhara, Y.; Kamimura, N.; Nakajima, M.; Hishiyama, S.; Hara, H.; Kasai, D.; Tsuji, Y.; Narita-Yamada, S.; Nakamura, S.; Katano, Y.; Fujita, N.; Katayama, Y.; Fukuda, M.; Kajita, S.; Masai, E.
Discovery of pinoresinol reductase genes in sphingomonads
Enzyme Microb. Technol.
52
38-43
2013
Novosphingobium aromaticivorans, Novosphingobium aromaticivorans DSM 12444, Sphingobium sp., Sphingobium sp. SYK-6
brenda
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
brenda
Dinkova-Kostova, A.T.; Gang, D.R.; Davin, L.B.; Bedgar, D.L.; Chu, A.; Lewis, N.G.
(+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase
J. Biol. Chem.
271
29473-29482
1996
Forsythia x intermedia
brenda
Nakatsubo, T.; Mizutani, M.; Suzuki, S.; Hattori, T.; Umezawa, T.
Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis
J. Biol. Chem.
283
15550-15557
2008
Arabidopsis thaliana, Arabidopsis thaliana (Q9FVQ6)
brenda
Ayella, A.K.; Trick, H.N.; Wang, W.
Enhancing lignan biosynthesis by over-expressing pinoresinol lariciresinol reductase in transgenic wheat
Mol. Nutr. Food Res.
51
1518-1526
2007
Forsythia x intermedia (P93143)
brenda
Katayama, T.; Davin, L.B.; Lewis, N.G.
An extraordinary accumulation of (-)-pinoresinol in cell-free extracts of Forsythia intermedia: evidence for enantiospecific reduction of (+)-pinoresinol
Phytochemistry
31
3875-3881
1992
Forsythia x intermedia
brenda
von Heimendahl, C.B.; Schaefer, K.M.; Eklund, P.; Sjoeholm, R.; Schmidt, T.J.; Fuss, E.
Pinoresinol-lariciresinol reductases with different stereospecificity from Linum album and Linum usitatissimum
Phytochemistry
66
1254-1263
2005
Linum album, Linum album (Q4R0I0)
brenda
Bayindir, U.; Alfermann, A.W.; Fuss, E.
Hinokinin biosynthesis in Linum corymbulosum Reichenb.
Plant J.
55
810-820
2008
Linum corymbulosum (B5KRH5), Linum corymbulosum
brenda
Hemmati, S.; von Heimendahl, C.B.; Klaes, M.; Alfermann, A.W.; Schmidt, T.J.; Fuss, E.
Pinoresinol-lariciresinol reductases with opposite enantiospecificity determine the enantiomeric composition of lignans in the different organs of Linum usitatissimum L.
Planta Med.
76
928-934
2010
Linum usitatissimum (E6Y2X0), Linum usitatissimum
brenda