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show all sequences of 1.1.1.195

Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase, key enzymes of monolignol biosynthesis

Pan, H.; Zhou, R.; Louie, G.V.; Muehlemann, J.K.; Bomati, E.K.; Bowman, M.E.; Dudareva, N.; Dixon, R.A.; Noel, J.P.; Wang, X.; Plant Cell 26, 3709-3727 (2014)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
potential exploitation of rationally engineered forms of CAD2 for the targeted modification of monolignol composition in transgenic plants
Medicago truncatula
Cloned(Commentary)
Commentary
Organism
diverse CAD or CAD-like genes in Medicago trunculata, phylogenetic analysis, recombinant expression of His-tagged Mt-CAD1 wild-type in Escherichia coli strain Rosetta2; diverse CAD or CAD-like genes in Medicago trunculata, phylogenetic analysis, recombinant expression of His-tagged Mt-CAD2 wild-type and mutants in Escherichia coli strain Rosetta2
Medicago truncatula
Engineering
Amino acid exchange
Commentary
Organism
F226A
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 4fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Medicago truncatula
K169A
site-directed mutagenesis, inactive mutant
Medicago truncatula
additional information
structure-based mutagenesis of Mt-CAD2 reveals and confirms the roles of key residues involved in catalysis and substrate binding and affords the engineering of catalytically active variants with increased turnover of sinapaldehyde
Medicago truncatula
S130A
site-directed mutagenesis, inactive mutant
Medicago truncatula
Y136F
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Medicago truncatula
Y136F/F226A
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Medicago truncatula
Y165A
site-directed mutagenesis, inactive mutant
Medicago truncatula
Y165F
site-directed mutagenesis, inactive mutant
Medicago truncatula
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0066
-
coniferyl aldehyde
wild-type Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.008
-
p-coumaryl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
0.0085
-
coniferyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
0.0094
-
p-coumaryl aldehyde
wild-type Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.0109
-
sinapyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
0.235
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
Medicago truncatula
0.279
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
Medicago truncatula
0.283
-
sinapyl aldehyde
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
Medicago truncatula
0.73
-
sinapyl aldehyde
wild-type Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
cinnamaldehyde + NADPH + H+
Medicago truncatula
-
cinnamyl alcohol + NADP+
-
-
r
cinnamyl alcohol + NADP+
Medicago truncatula
-
cinnamaldehyde + NADPH + H+
-
-
r
coniferyl alcohol + NADP+
Medicago truncatula
-
coniferyl aldehyde + NADPH + H+
-
-
r
coniferyl aldehyde + NADPH + H+
Medicago truncatula
-
coniferyl alcohol + NADP+
-
-
r
p-coumaryl alcohol + NADP+
Medicago truncatula
-
p-coumaryl aldehyde + NADPH + H+
-
-
r
sinapyl alcohol + NADP+
Medicago truncatula
-
sinapyl aldehyde + NADPH + H+
-
-
r
sinapyl aldehyde + NADPH + H+
Medicago truncatula
-
sinapyl alcohol + NADP+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Medicago truncatula
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant Mt-CAD2 enzymes by nickel affinity chromatography, tag cleavage by thrombin, benzamidine affinity chromatography to remove thrombin, and gel filtration; recombinant His-tagged wild-type Mt-CAD1 enzyme by nickel affinity chromatography, tag cleavage by thrombin, benzamidine affinity chromatography to remove thrombin, and gel filtration
Medicago truncatula
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cinnamaldehyde + NADPH + H+
-
741161
Medicago truncatula
cinnamyl alcohol + NADP+
-
-
-
r
cinnamyl alcohol + NADP+
-
741161
Medicago truncatula
cinnamaldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
-
741161
Medicago truncatula
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH + H+
-
741161
Medicago truncatula
coniferyl alcohol + NADP+
-
-
-
r
additional information
the enzyme Mt-CAD2 shows low activity with all substrates and compared to the activities of Mt-CAD1, substrate binding and specificity of Mt-CAD2, overview
741161
Medicago truncatula
?
-
-
-
-
p-coumaryl alcohol + NADP+
-
741161
Medicago truncatula
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
-
741161
Medicago truncatula
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl aldehyde + NADPH + H+
-
741161
Medicago truncatula
sinapyl alcohol + NADP+
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
alpha-helical and beta-strand segments of Mt-CAD2, modelling, overview
Medicago truncatula
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
aldehyde reduction, assay at
Medicago truncatula
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.024
-
sinapyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.039
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
Medicago truncatula
0.044
-
sinapyl aldehyde
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
Medicago truncatula
0.083
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
Medicago truncatula
0.1
-
coniferyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.46
-
p-coumaryl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
9.1
-
coniferyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
10.2
-
sinapyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
15.6
-
p-coumaryl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.25
-
aldehyde reduction, assay at
Medicago truncatula
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Medicago truncatula
NADPH
-
Medicago truncatula
Application (protein specific)
Application
Commentary
Organism
synthesis
potential exploitation of rationally engineered forms of CAD2 for the targeted modification of monolignol composition in transgenic plants
Medicago truncatula
Cloned(Commentary) (protein specific)
Commentary
Organism
diverse CAD or CAD-like genes in Medicago trunculata, phylogenetic analysis, recombinant expression of His-tagged Mt-CAD1 wild-type in Escherichia coli strain Rosetta2; diverse CAD or CAD-like genes in Medicago trunculata, phylogenetic analysis, recombinant expression of His-tagged Mt-CAD2 wild-type and mutants in Escherichia coli strain Rosetta2
Medicago truncatula
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Medicago truncatula
NADPH
-
Medicago truncatula
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F226A
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 4fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Medicago truncatula
K169A
site-directed mutagenesis, inactive mutant
Medicago truncatula
additional information
structure-based mutagenesis of Mt-CAD2 reveals and confirms the roles of key residues involved in catalysis and substrate binding and affords the engineering of catalytically active variants with increased turnover of sinapaldehyde
Medicago truncatula
S130A
site-directed mutagenesis, inactive mutant
Medicago truncatula
Y136F
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Medicago truncatula
Y136F/F226A
site-directed mutagenesis, the mutation leads to an enlarged phenolic binding site resulting in a 10fold increase in activity with sinapaldehyde, which in comparison to the smaller coumaraldehyde and coniferaldehyde substrates is disfavored by wild-type CAD2
Medicago truncatula
Y165A
site-directed mutagenesis, inactive mutant
Medicago truncatula
Y165F
site-directed mutagenesis, inactive mutant
Medicago truncatula
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0066
-
coniferyl aldehyde
wild-type Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.008
-
p-coumaryl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
0.0085
-
coniferyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
0.0094
-
p-coumaryl aldehyde
wild-type Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.0109
-
sinapyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
0.235
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
Medicago truncatula
0.279
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
Medicago truncatula
0.283
-
sinapyl aldehyde
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
Medicago truncatula
0.73
-
sinapyl aldehyde
wild-type Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
cinnamaldehyde + NADPH + H+
Medicago truncatula
-
cinnamyl alcohol + NADP+
-
-
r
cinnamyl alcohol + NADP+
Medicago truncatula
-
cinnamaldehyde + NADPH + H+
-
-
r
coniferyl alcohol + NADP+
Medicago truncatula
-
coniferyl aldehyde + NADPH + H+
-
-
r
coniferyl aldehyde + NADPH + H+
Medicago truncatula
-
coniferyl alcohol + NADP+
-
-
r
p-coumaryl alcohol + NADP+
Medicago truncatula
-
p-coumaryl aldehyde + NADPH + H+
-
-
r
sinapyl alcohol + NADP+
Medicago truncatula
-
sinapyl aldehyde + NADPH + H+
-
-
r
sinapyl aldehyde + NADPH + H+
Medicago truncatula
-
sinapyl alcohol + NADP+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant Mt-CAD2 enzymes by nickel affinity chromatography, tag cleavage by thrombin, benzamidine affinity chromatography to remove thrombin, and gel filtration; recombinant His-tagged wild-type Mt-CAD1 enzyme by nickel affinity chromatography, tag cleavage by thrombin, benzamidine affinity chromatography to remove thrombin, and gel filtration
Medicago truncatula
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cinnamaldehyde + NADPH + H+
-
741161
Medicago truncatula
cinnamyl alcohol + NADP+
-
-
-
r
cinnamyl alcohol + NADP+
-
741161
Medicago truncatula
cinnamaldehyde + NADPH + H+
-
-
-
r
coniferyl alcohol + NADP+
-
741161
Medicago truncatula
coniferyl aldehyde + NADPH + H+
-
-
-
r
coniferyl aldehyde + NADPH + H+
-
741161
Medicago truncatula
coniferyl alcohol + NADP+
-
-
-
r
additional information
the enzyme Mt-CAD2 shows low activity with all substrates and compared to the activities of Mt-CAD1, substrate binding and specificity of Mt-CAD2, overview
741161
Medicago truncatula
?
-
-
-
-
p-coumaryl alcohol + NADP+
-
741161
Medicago truncatula
p-coumaryl aldehyde + NADPH + H+
-
-
-
r
sinapyl alcohol + NADP+
-
741161
Medicago truncatula
sinapyl aldehyde + NADPH + H+
-
-
-
r
sinapyl aldehyde + NADPH + H+
-
741161
Medicago truncatula
sinapyl alcohol + NADP+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
alpha-helical and beta-strand segments of Mt-CAD2, modelling, overview
Medicago truncatula
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
aldehyde reduction, assay at
Medicago truncatula
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.024
-
sinapyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.039
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
Medicago truncatula
0.044
-
sinapyl aldehyde
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
Medicago truncatula
0.083
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
Medicago truncatula
0.1
-
coniferyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.46
-
p-coumaryl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
9.1
-
coniferyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
10.2
-
sinapyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
15.6
-
p-coumaryl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.25
-
aldehyde reduction, assay at
Medicago truncatula
General Information
General Information
Commentary
Organism
evolution
enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1; enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily, the SDR108E family together with a SDR115E daughter branch. Mt-CAD2 resides in the flowering plant phenylacetaldehyde-reductase subgroup. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1
Medicago truncatula
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
Medicago truncatula
additional information
the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Mmolecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, structural modeling of Mt-CAD1, overview; the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Molecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, binding pockets for NADP(H) co-substrate and phenolic-aldehyde substrate in Mt-CAD2, overview
Medicago truncatula
General Information (protein specific)
General Information
Commentary
Organism
evolution
enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1; enzyme CAD2 is a member of the short-chain dehydrogenase/reductase (SDR) superfamily, the SDR108E family together with a SDR115E daughter branch. Mt-CAD2 resides in the flowering plant phenylacetaldehyde-reductase subgroup. There are two CADs in Medicago truncatula, CAD1 and CAD2, which represent a classical and an atypical CAD belonging to the MDR and SDR families, respectively. Mt-CAD1 is highly active with all three substrates, coumaraldehyde, coniferaldehyde, and sinapaldehyde. By contrast, Mt-CAD2 exhibits relatively modest activity. The turnover rates (kcat) with coumaraldehyde, coniferaldehyde, and sinapaldehyde are only 3, 1, and 0.25%, respectively, of those for Mt-CAD1
Medicago truncatula
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
Medicago truncatula
additional information
the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Mmolecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, structural modeling of Mt-CAD1, overview; the reaction mechanism involves a canonical SDR catalytic triad. Enzyme CAD2 shows substantial conformational flexibility, which plays an important role in the establishment of catalytically productive complexes of the enzyme with its NADPH and phenolic substrates. Molecular modeling and docking studies elucidate the specific interactions of Mt-CAD1 and Mt-CAD2 with NADPH and substrates, binding pockets for NADP(H) co-substrate and phenolic-aldehyde substrate in Mt-CAD2, overview
Medicago truncatula
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0328
-
sinapyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.14
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
Medicago truncatula
0.156
-
sinapyl aldehyde
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
Medicago truncatula
0.354
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
Medicago truncatula
15.3
-
coniferyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
48.9
-
p-coumaryl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
926
-
sinapyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
1070
-
coniferyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
1950
-
p-coumaryl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0328
-
sinapyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
0.14
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F, pH and temperature not specified in the publication
Medicago truncatula
0.156
-
sinapyl aldehyde
Mt-CAD2 mutant F226A, pH and temperature not specified in the publication
Medicago truncatula
0.354
-
sinapyl aldehyde
Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication
Medicago truncatula
15.3
-
coniferyl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
48.9
-
p-coumaryl aldehyde
Mt-CAD2, pH and temperature not specified in the publication
Medicago truncatula
926
-
sinapyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
1070
-
coniferyl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
1950
-
p-coumaryl aldehyde
Mt-CAD1, pH and temperature not specified in the publication
Medicago truncatula
Other publictions for EC 1.1.1.195
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738304
Rong
A wheat cinnamyl alcohol dehyd ...
Triticum aestivum
Front. Plant Sci.
7
1723
2016
-
-
1
-
-
-
-
2
1
1
-
2
-
5
-
-
-
-
-
3
1
-
6
2
-
-
-
-
-
-
-
3
-
1
-
-
-
2
4
-
-
-
-
-
-
2
1
1
-
2
-
-
-
-
-
3
1
-
6
2
-
-
-
-
-
-
-
1
1
3
4
2
-
-
739331
Bhattacharyya
Transcriptome-wide identificat ...
Sinopodophyllum hexandrum
Plant Mol. Biol.
92
1-23
2016
-
-
1
-
1
-
-
8
-
1
4
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5
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Vidal
Characterization of an alcohol ...
Synechocystis sp.
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Bhuiyan
Gene expression profiling and ...
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Kovacik
Phenolic metabolism of Matrica ...
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700730
Bedon
Sequence analysis and function ...
Picea glauca, Pinus taeda
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Li
FLEXIBLE CULM 1 encoding a cin ...
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Sattler
A nonsense mutation in a cinna ...
Sorghum bicolor
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Saidi
Thigmomorphogenesis in Solanum ...
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Luo
Use of 1-methylcyclopropene fo ...
Phyllostachys praecox
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Nur Fariza
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Extensive DNA sequence variati ...
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Tsuruta
-
Isolation and characterization ...
Sorghum bicolor
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688654
Chen
Root and vascular tissue-speci ...
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689105
Ali
Methyl jasmonate and salicylic ...
Panax ginseng
Molecules
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2007
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689418
Jourdes
Plant cell walls are enfeebled ...
Arabidopsis thaliana
Phytochemistry
68
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2007
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689419
Kim
Expression of cinnamyl alcohol ...
Arabidopsis thaliana
Phytochemistry
68
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2007
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Prats
Differential effects of phenyl ...
Hordeum vulgare, Triticum aestivum
Phytopathology
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1578-1583
2007
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689537
Dauwe
Molecular phenotyping of ligni ...
Nicotiana tabacum
Plant J.
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Youn
Crystal structures and catalyt ...
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670596
Zhang
Gold-hull-and-internode2-gene ...
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Ali
Phenolics metabolism and ligni ...
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Hano
Differential accumulation of m ...
Linum usitatissimum
Planta
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Eudes
Evidence for a role of AtCAD 1 ...
Arabidopsis thaliana
Planta
225
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670974
Moeller
Lignification in cell cultures ...
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1
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1
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668545
Mee
Characterization of cinnamyl a ...
Helicobacter pylori
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1255-1264
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1
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1
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13
1
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670531
Sibout
Cinnamyl alcohol dehydrogenase ...
Arabidopsis thaliana
Plant Cell
17
2059-2076
2005
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1
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1
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1
2
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1
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2
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1
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3
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670569
Damiani
Metabolite profiling reveals a ...
Nicotiana tabacum
Plant Mol. Biol.
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753-769
2005
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1
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1
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3
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4
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2
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4
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4
4
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670603
Moeller
Gene silencing of cinnamyl alc ...
Pinus radiata
Plant Physiol. Biochem.
43
1061-1066
2005
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1
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1
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5
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1
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1
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1
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3
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1
-
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-
-
-
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-
-
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670609
Ali
CO2-induced total phenolics in ...
Panax ginseng
Plant Physiol. Biochem.
43
449-457
2005
1
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1
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1
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2
1
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-
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656540
Valencia
Apo and Holo structures of an ...
Saccharomyces cerevisiae
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2004
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1
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1
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1
1
1
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1
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1
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1
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-
-
-
-
-
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656769
Valerio
Down regulation of cinnamyl al ...
Eucalyptus camaldulensis
Mol. Breed.
12
157-167
2003
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1
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1
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1
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1
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1
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1
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1
1
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1
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1
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1
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656926
Ruelland
-
Cellular and subcellular local ...
Saccharum officinarum
Physiol. Plant.
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93-99
2003
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1
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1
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4
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2
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657055
Sibout
Expression pattern of two para ...
Arabidopsis thaliana
Plant Physiol.
132
848-860
2003
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1
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1
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1
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5
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3
1
1
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1
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656400
Blanco-Portales
Cloning, expression and immuno ...
Fragaria x ananassa
J. Exp. Bot.
53
1723-1734
2002
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1
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6
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9
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1
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9
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2
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1
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1
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347820
Mitchell
-
Differential induction of cinn ...
Triticum aestivum
Planta
208
31-37
1999
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10
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1
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3
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347822
Samaj
Immunolocalization of cinnamyl ...
Populus tremula x Populus alba
Planta
204
437-443
1998
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-
-
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4
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10
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10
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347823
Goffner
A novel aromatic alcohol dehyd ...
Eucalyptus gunnii
Plant Mol. Biol.
36
755-765
1998
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1
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1
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5
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3
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347816
Logemann
A novel type of pathogen defen ...
Petroselinum crispum
Biol. Chem.
378
909-913
1997
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1
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6
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1
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3
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7
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7
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347817
Nakashima
-
Immunocytochemical localizatio ...
Zinnia elegans
Plant Cell Physiol.
38
113-123
1997
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2
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1
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347815
Lauvergeat
Site-directed mutagenesis of a ...
Eucalyptus gunnii
Biochemistry
34
12426-12434
1995
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1
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1
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2
5
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4
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3
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3
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3
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5
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1
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4
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3
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3
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347821
Grima-Pettenati
Purification and characterizat ...
Phaseolus vulgaris
Phytochemistry
37
941-947
1994
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-
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11
-
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2
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2
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1
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1
1
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3
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11
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1
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3
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-
347814
McKie
A molecular model for cinnamyl ...
Eucalyptus sp.
Biochim. Biophys. Acta
1202
61-69
1993
-
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1
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1
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1
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1
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347819
Hibino
Purification and partial seque ...
Aralia cordata
Phytochemistry
32
565-567
1993
-
-
-
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-
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6
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2
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2
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1
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1
1
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2
1
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2
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2
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6
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1
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1
1
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2
1
-
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-
347818
O'Malley
Purification, characterization ...
Pinus taeda
Plant Physiol.
98
1364-1371
1992
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1
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1
5
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2
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3
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1
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1
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2
1
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3
1
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2
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-
347802
Kush
Laticifer-specific gene expres ...
Hevea brasiliensis
Proc. Natl. Acad. Sci. USA
87
1787-1790
1990
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288231
Grima-Pettenati
-
Stimulation of lignification i ...
Vigna mungo
Plant Sci.
61
179-188
1989
-
-
-
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1
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1
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347804
Walter
Cinnamyl-alcohol dehydrogenase ...
Phaseolus vulgaris
Proc. Natl. Acad. Sci. USA
85
5546-5550
1988
-
-
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1
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1
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-
347805
Grand
Rapid induction by fungal elic ...
Phaseolus vulgaris
Eur. J. Biochem.
169
73-77
1987
-
-
-
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1
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1
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1
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1
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-
347806
Moerschbacher
-
An elicitor of the hypersensit ...
Triticum aestivum
Z. Naturforsch. C
41
839-844
1986
-
-
-
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-
288228
Sarni
Purification and properties of ...
Populus x canadensis
Eur. J. Biochem.
139
259-265
1984
-
-
-
-
-
4
-
4
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1
2
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2
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1
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1
1
1
3
1
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2
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1
1
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1
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4
-
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4
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1
2
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1
-
1
1
1
3
1
-
-
-
-
2
-
1
-
-
-
-
-
-
-
347808
Kutsuki
-
Regulatory role of cinnamyl al ...
Cryptomeria japonica, Erythrina crista-galli, Ginkgo biloba, Liriodendron tulipifera, Metasequoia glyptostroboides, Pinus thunbergii, Platycladus orientalis, Populus x canadensis, Prunus persica, Prunus yedoensis, Robinia pseudoacacia
Phytochemistry
21
19-23
1982
-
-
-
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-
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-
5
-
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-
11
-
11
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1
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1
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35
-
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11
-
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11
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5
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11
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1
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1
-
35
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
288233
Luderitz
Enzymic synthesis of lignin pr ...
Picea abies
Eur. J. Biochem.
119
115-124
1981
-
-
-
-
-
2
-
1
-
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1
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1
1
1
3
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1
1
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1
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1
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2
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1
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1
1
1
3
-
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1
1
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-
-
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-
-
-
-
347810
Kutsuki
Activities of some enzymes of ...
Metasequoia glyptostroboides, Platycladus orientalis, Robinia pseudoacacia
Planta
152
365-368
1981
-
-
-
-
-
-
-
-
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6
-
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3
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3
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-
-
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-
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-
347812
Wyrambik
Enzymic synthesis of lignin pr ...
Glycine max
Eur. J. Biochem.
97
503-509
1979
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
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1
1
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2
1
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1
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-
1
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1
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-
-
-
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-
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1
-
2
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347813
Klischies
-
Stereospecificity of cinnamoyl ...
Forsythia suspensa
Phytochemistry
17
1523-1525
1978
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
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1
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-
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1
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-
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-
1
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1
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1
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-
-
-
-
-
-
-
-
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-
-
-
-
-
347801
Wyrambik
Purification and properties of ...
Glycine max
Eur. J. Biochem.
59
9-15
1975
-
-
-
-
-
-
-
12
-
-
1
-
-
2
-
-
1
-
-
2
1
1
5
-
-
-
-
-
2
2
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
12
-
-
1
-
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-
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1
-
2
1
1
5
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
347811
Mansell
-
Purification and properties of ...
Abies nobilis, Acer campestre, Acer saccharinum, Athyrium filix-femina, Atrichum undulatum, Avena sativa, Betula pendula, Cichorium endivia, Corylus sp., Daucus carota, Equisetum arvense, Equisetum palustre, Forsythia suspensa, Ginkgo biloba, Helianthus annuus, Heracleum mantegazzianum, Hordeum sp., Ilex aquifolium, Larix kaempferi, Ligustrum vulgare, Linum usitatissimum, Liriodendron tulipifera, Metasequoia glyptostroboides, Morinda citrifolia, Nephrolepis exaltata, Picea abies, Pinus peuce, Pinus strobus, Pisum sativum, Platanus x hispanica, Populus nigra, Populus tremula, Prunus serotina, Pseudotsuga menziesii, Pteris cretica, Pteris wimsetti, Quercus robur, Quercus rubra, Salix alba, Salvinia natans, Sambucus racemosa, Secale cereale, Selaginella kraussiana, Selaginella martensii, Sorbus aucuparia, Sorbus domestica, Sphagnum sp., Syringa vulgaris, Taxus baccata, Thuja plicata, Woodwardia radicans, Zea mays
Phytochemistry
13
2427-2435
1974
-
-
-
-
-
2
-
5
-
-
1
-
-
52
-
-
1
1
-
1
52
1
16
-
1
-
1
-
2
-
2
1
-
-
-
-
-
-
1
-
-
2
-
-
-
5
-
-
1
-
-
-
-
1
-
1
52
1
16
-
1
-
1
-
2
-
2
-
-
-
-
-
-
-