BRENDA - Enzyme Database show
show all sequences of 1.1.1.282

Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles

Ossipov, V.; Bonner, C.; Ossipova, S.; Jensen, R.; Plant Physiol. Biochem. 38, 923-928 (2000)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
L-quinate
competitive inhibitor with respect to shikimate
Pinus taeda
shikimate
competitive inhibitor with respect to L-quinate
Pinus taeda
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
NADP+
pH 10, 20°C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
0.005
0.012
NADPH
pH 10, 20°C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
0.007
-
NADP+
pH 10, 20°C, cosubstrate L-quinate, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
0.7
0.8
shikimate
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
1
-
dehydroquinate
pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase
Pinus taeda
3.4
3.6
L-quinate
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
5.3
-
dehydroquinate
pH 10, 20°C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase
Pinus taeda
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
Pinus taeda
53000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
Pinus taeda
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroquinate + NADPH + H+
Pinus taeda
may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
L-quinate + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pinus taeda
-
20 years old
-
Purification (Commentary)
Commentary
Organism
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2
Pinus taeda
Source Tissue
Source Tissue
Commentary
Organism
Textmining
needle
from current-year shoots of 20 years old trees, the youngest basal parts of needles
Pinus taeda
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pinus taeda
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroquinate + NADPH + H+
may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
657079
Pinus taeda
L-quinate + NADP+
-
-
-
?
L-quinate + NADP+
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold greater with quinate than with shikimate
657079
Pinus taeda
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NADP+
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold lower with shikimate than with quinate
657079
Pinus taeda
3-dehydroshikimate + NADPH + H+
-
-
-
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Pinus taeda
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.7
-
back reaction, dehydroquinate or dehydroshikimate and NADPH as substrates
Pinus taeda
10.3
-
quinate or shikimate and NADP+ as substrates
Pinus taeda
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Pinus taeda
NADPH
-
Pinus taeda
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Pinus taeda
NADPH
-
Pinus taeda
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-quinate
competitive inhibitor with respect to shikimate
Pinus taeda
shikimate
competitive inhibitor with respect to L-quinate
Pinus taeda
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
NADP+
pH 10, 20°C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
0.005
0.012
NADPH
pH 10, 20°C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
0.007
-
NADP+
pH 10, 20°C, cosubstrate L-quinate, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
0.7
0.8
shikimate
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
1
-
dehydroquinate
pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase
Pinus taeda
3.4
3.6
L-quinate
pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase
Pinus taeda
5.3
-
dehydroquinate
pH 10, 20°C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase
Pinus taeda
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
Pinus taeda
53000
-
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration
Pinus taeda
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroquinate + NADPH + H+
Pinus taeda
may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
L-quinate + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2
Pinus taeda
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
needle
from current-year shoots of 20 years old trees, the youngest basal parts of needles
Pinus taeda
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pinus taeda
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroquinate + NADPH + H+
may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid
657079
Pinus taeda
L-quinate + NADP+
-
-
-
?
L-quinate + NADP+
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold greater with quinate than with shikimate
657079
Pinus taeda
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NADP+
both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold lower with shikimate than with quinate
657079
Pinus taeda
3-dehydroshikimate + NADPH + H+
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Pinus taeda
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.7
-
back reaction, dehydroquinate or dehydroshikimate and NADPH as substrates
Pinus taeda
10.3
-
quinate or shikimate and NADP+ as substrates
Pinus taeda
Other publictions for EC 1.1.1.282
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)
740881
Garcia
The role of the ydiB gene, whi ...
Escherichia coli, Escherichia coli JM101
J. Mol. Microbiol. Biotechnol.
27
11-21
2016
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1
1
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1
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6
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10
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6
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2
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1
2
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1
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6
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6
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739956
Peek
The shikimate dehydrogenase fa ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Arch. Biochem. Biophys.
566
85-99
2015
-
1
1
1
-
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5
-
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6
-
4
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2
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9
1
1
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4
2
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4
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2
2
4
2
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5
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6
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9
2
2
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4
2
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4
8
-
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740724
Guo
Molecular characterization of ...
Populus trichocarpa, Populus trichocarpa Nisqually-1
J. Biol. Chem.
289
23846-23858
2014
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1
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5
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3
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5
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1
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7
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3
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1
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1
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4
4
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724089
Kubota
Characterization of shikimate ...
Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
97
8139-8149
2013
-
-
1
-
1
-
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6
-
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2
3
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1
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1
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5
1
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5
2
1
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3
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1
3
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1
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6
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2
3
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1
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5
1
-
-
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5
2
1
-
-
1
1
1
1
5
5
727115
Höppner
Enzyme-substrate complexes of ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Biol. Chem.
394
1505-1516
2013
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1
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8
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5
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5
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1
1
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8
2
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1
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5
1
1
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8
2
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1
1
-
8
8
740100
Peek
Insights into the function of ...
Pseudomonas putida, Pseudomonas putida KT 2240
Biochim. Biophys. Acta
1834
516-523
2013
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1
1
4
-
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6
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1
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4
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4
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1
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6
1
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6
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1
3
1
4
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1
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4
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1
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6
1
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6
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1
1
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6
6
694093
Singh
A phylogenomic analysis of the ...
Pseudomonas putida KT2440
Mol. Biol. Evol.
25
2221-2232
2008
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1
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-
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4
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3
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1
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3
9
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4
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1
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3
3
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4
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3
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3
9
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4
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667700
Singh
Structure of Arabidopsis dehyd ...
Arabidopsis thaliana
Biochemistry
45
10406
2006
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1
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656292
Lindner
Site-directed mutagenesis of t ...
Escherichia coli
J. Biol. Chem.
280
7162-7169
2005
-
2
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8
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28
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3
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2
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1
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29
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4
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8
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28
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3
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4
1
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29
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669328
Singh
Crystal structure of a novel s ...
Enterococcus faecalis, Enterococcus faecium, Escherichia coli, Haemophilus influenzae, Lactobacillus plantarum, Listeria monocytogenes, Salmonella enterica subsp. enterica serovar Typhimurium, Shigella flexneri, Streptococcus pyogenes
J. Biol. Chem.
280
17101-17108
2005
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9
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9
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644536
Michel
Structures of shikimate dehydr ...
Escherichia coli
J. Biol. Chem.
278
19463-19472
2003
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1
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8
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1
1
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4
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2
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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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3
1
1
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6
1
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644537
Benach
The 2.3-Å crystal structure o ...
Escherichia coli
J. Biol. Chem.
278
19176-19182
2003
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1
1
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657079
Ossipov
-
Broad-specificity quinate (shi ...
Pinus taeda
Plant Physiol. Biochem.
38
923-928
2000
-
-
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2
7
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2
1
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1
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1
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1
1
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3
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1
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2
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2
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2
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2
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7
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2
1
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1
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1
1
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3
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1
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2
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654384
Bruce
-
Hydroaromatic metabolism in Rh ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous N75
Arch. Microbiol.
154
179-186
1990
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8
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2
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5
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2
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16
1
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1
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1
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7
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7
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2
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1
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16
1
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1
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2
1
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654912
Osipov
-
The role of quinate dehydrogen ...
Larix sibirica, Pinus sylvestris
Biokhimiya
51
230-236
1986
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2
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286356
Barea
Purification and characterizat ...
Neurospora crassa
Biochim. Biophys. Acta
524
1-14
1978
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