BRENDA - Enzyme Database
show all sequences of 1.1.1.25

The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework

Peek, J.; Christendat, D.; Arch. Biochem. Biophys. 566, 85-99 (2015)

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Aquifex aeolicus
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Archaeoglobus fulgidus
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Aspergillus nidulans
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Corynebacterium glutamicum
drug development
the essential enzyme is a potential target for antimicrobials
Escherichia coli
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Helicobacter pylori
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Mycobacterium tuberculosis
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Pseudomonas putida
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Staphylococcus aureus
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Staphylococcus epidermidis
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Toxoplasma gondii
Cloned(Commentary)
Cloned (Commentary)
Organism
gene aroE, recombinant expression
Corynebacterium glutamicum
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates
Arabidopsis thaliana
crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO
Staphylococcus epidermidis
crystal structure determination of the apoenzyme, PDB ID 4OMU
Pseudomonas putida
determination of diverse crystal structures with apoenzyme, or enzyme in binary or ternary complexes
Helicobacter pylori
Engineering
Protein Variants
Commentary
Organism
additional information
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
Staphylococcus epidermidis
Q237A
site-directed mutagenesis
Helicobacter pylori
Q237K
site-directed mutagenesis
Helicobacter pylori
Q237N
site-directed mutagenesis
Helicobacter pylori
Y210A
site-directed mutagenesis
Helicobacter pylori
Y210S
site-directed mutagenesis
Helicobacter pylori
Inhibitors
Inhibitors
Commentary
Organism
Structure
curcumin
a noncompetitive inhibitor
Helicobacter pylori
additional information
inhibitor screening
Helicobacter pylori
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0091
-
NADP+
pH 8.8, 25°C, with shikimate
Toxoplasma gondii
0.0135
-
NADP+
with shikimate, pH 7.0, 25°C
Aspergillus nidulans
0.022
-
NADP+
pH 7.0, 25°C, with shikimate
Mycobacterium tuberculosis
0.03
-
shikimate
pH 9.0, 25°C, with NADP+
Mycobacterium tuberculosis
0.031
-
3-dehydroshikimate
pH 7.0, 25°C, with NADPH
Mycobacterium tuberculosis
0.031
-
NADPH
pH 7.0, 25°C, with 3-dehydroshikimate
Mycobacterium tuberculosis
0.0375
-
shikimate
pH not specified in the publication, 25°C, with NADP+
Staphylococcus aureus
0.0424
-
NADP+
with shikimate, pH 9.0, 25°C
Aquifex aeolicus
0.0425
-
shikimate
with NADP+, pH 9.0, 25°C
Aquifex aeolicus
0.0426
-
NADP+
pH not specified in the publication, 25°C, with shikimate
Staphylococcus aureus
0.0502
-
shikimate
pH 7.0, 25°C, with NADP+
Mycobacterium tuberculosis
0.0527
-
shikimate
pH 8.8, 25°C, with NADP+
Toxoplasma gondii
0.055
-
NADP+
pH 8.8, 25°C, with shikimate
Pseudomonas putida
0.056
-
NADP+
with shikimate, pH 9.0, 20°C
Escherichia coli
0.063
-
NADP+
pH 9.0, 25°C, with shikimate
Mycobacterium tuberculosis
0.065
-
shikimate
with NADP+, pH 9.0, 20°C
Escherichia coli
0.073
-
shikimate
pH 7.0, 25°C, with NADP+
Staphylococcus epidermidis
0.1
-
NADP+
pH 7.0, 25°C, with shikimate
Staphylococcus epidermidis
0.131
-
NADP+
pH 8.8, 22°C, with shikimate
Arabidopsis thaliana
0.14
-
shikimate
with NADP+, pH 9.0, 30°C
Corynebacterium glutamicum
0.148
-
shikimate
with NADP+, pH 8.0, 25°C
Helicobacter pylori
0.17
-
shikimate
with NADP+, pH 7.3, 87°C
Archaeoglobus fulgidus
0.178
-
shikimate
pH 8.8, 25°C, with NADP+
Pseudomonas putida
0.182
-
NADP+
with shikimate, pH 8.0, 25°C
Helicobacter pylori
0.19
-
NADP+
with shikimate, pH 7.3, 87°C
Archaeoglobus fulgidus
0.223
-
shikimate
pH 8.5, 22°C, with NADP+, isozyme Poptr1
Populus trichocarpa
0.272
-
3-dehydroshikimate
with NADPH, pH 8.6, 30°C
Corynebacterium glutamicum
0.311
-
shikimate
with NADP+, pH 7.0, 25°C
Aspergillus nidulans
0.346
-
shikimate
pH 8.5, 22°C, with NADP+, isozyme Poptr5
Populus trichocarpa
0.685
-
shikimate
pH 8.8, 22°C, with NADP+
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3-dehydroshikimate + NADPH
Populus trichocarpa
-
shikimate + NADP+
-
-
r
3-dehydroshikimate + NADPH
Arabidopsis thaliana
-
shikimate + NADP+
-
-
r
shikimate + NADP+
Staphylococcus aureus
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Escherichia coli
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Helicobacter pylori
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Aquifex aeolicus
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Aspergillus nidulans
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Archaeoglobus fulgidus
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Corynebacterium glutamicum
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Mycobacterium tuberculosis
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Staphylococcus epidermidis
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Toxoplasma gondii
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Archaeoglobus fulgidus ATCC 49558
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Aspergillus nidulans FGSC A4
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Staphylococcus epidermidis ATCC 35984
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida KT 2240
-
3-dehydroshikimate + NADPH + H+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Aquifex aeolicus
O67049
-
-
Arabidopsis thaliana
Q9SQT8
-
-
Archaeoglobus fulgidus
O27957
-
-
Archaeoglobus fulgidus ATCC 49558
O27957
-
-
Aspergillus nidulans
P07547
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
-
Aspergillus nidulans FGSC A4
P07547
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
-
Corynebacterium glutamicum
A4QB65
-
-
Escherichia coli
-
-
-
Helicobacter pylori
-
-
-
Mycobacterium tuberculosis
A0A1K3RIC7
-
-
Populus trichocarpa
-
-
-
Pseudomonas putida
Q88IJ7
-
-
Pseudomonas putida KT 2240
Q88IJ7
-
-
Staphylococcus aureus
-
-
-
Staphylococcus epidermidis
Q5HNV1
-
-
Staphylococcus epidermidis ATCC 35984
Q5HNV1
-
-
Toxoplasma gondii
Q6W3D0
shikimate dehydrogenase as part of the pentafunctional AROM polypeptide
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
732
-
pH 7.3, 87°C
Archaeoglobus fulgidus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3-dehydroshikimate + NADPH
-
739956
Populus trichocarpa
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH
-
739956
Arabidopsis thaliana
shikimate + NADP+
-
-
-
r
additional information
no activity with quinate
739956
Helicobacter pylori
?
-
-
-
-
additional information
no activity with quinate
739956
Pseudomonas putida
?
-
-
-
-
additional information
no activity with quinate
739956
Archaeoglobus fulgidus
?
-
-
-
-
additional information
no activity with quinate
739956
Staphylococcus epidermidis
?
-
-
-
-
additional information
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
739956
Populus trichocarpa
?
-
-
-
-
additional information
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
739956
Arabidopsis thaliana
?
-
-
-
-
additional information
the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate
739956
Toxoplasma gondii
?
-
-
-
-
additional information
no activity with quinate
739956
Archaeoglobus fulgidus ATCC 49558
?
-
-
-
-
additional information
no activity with quinate
739956
Staphylococcus epidermidis ATCC 35984
?
-
-
-
-
additional information
no activity with quinate
739956
Pseudomonas putida KT 2240
?
-
-
-
-
shikimate + NADP+
-
739956
Staphylococcus aureus
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Escherichia coli
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Helicobacter pylori
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Aquifex aeolicus
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Pseudomonas putida
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Aspergillus nidulans
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Archaeoglobus fulgidus
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Corynebacterium glutamicum
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Mycobacterium tuberculosis
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Staphylococcus epidermidis
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Toxoplasma gondii
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Archaeoglobus fulgidus ATCC 49558
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Aspergillus nidulans FGSC A4
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Staphylococcus epidermidis ATCC 35984
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Pseudomonas putida KT 2240
3-dehydroshikimate + NADPH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
-
Corynebacterium glutamicum
dimer
-
Mycobacterium tuberculosis
monomer
in solution
Arabidopsis thaliana
monomer
-
Escherichia coli
monomer
-
Staphylococcus epidermidis
More
SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring
Aquifex aeolicus
More
the SDH domain is connected via its N-terminus to the DHQ module
Arabidopsis thaliana
Synonyms
Synonyms
Commentary
Organism
AroE
-
Aquifex aeolicus
AroE
-
Archaeoglobus fulgidus
dehydroquinate dehydratase/shikimate dehydrogenase
-
Arabidopsis thaliana
dehydroquinate dehydratase/shikimate dehydrogenase
-
Populus trichocarpa
DQD/SDH
-
Arabidopsis thaliana
DQD/SDH
-
Populus trichocarpa
SDH
-
Aquifex aeolicus
SDH
-
Archaeoglobus fulgidus
SDH
-
Aspergillus nidulans
SDH
-
Corynebacterium glutamicum
SDH
-
Escherichia coli
SDH
-
Helicobacter pylori
SDH
-
Pseudomonas putida
SDH
-
Staphylococcus epidermidis
SDH
-
Toxoplasma gondii
SDH
-
Staphylococcus aureus
SDH
-
Mycobacterium tuberculosis
YdiB
-
Escherichia coli
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Escherichia coli
22
-
shikimate oxidation assay at room temperature
Arabidopsis thaliana
22
-
assay at room temperature
Populus trichocarpa
25
-
assay at
Aquifex aeolicus
25
-
assay at
Aspergillus nidulans
25
-
assay at
Mycobacterium tuberculosis
25
-
assay at
Pseudomonas putida
25
-
assay at
Staphylococcus aureus
25
-
assay at
Staphylococcus epidermidis
25
-
assay at
Toxoplasma gondii
30
-
assay at
Corynebacterium glutamicum
87
-
assay at
Archaeoglobus fulgidus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.5
-
shikimate
with NADP+, pH 7.0, 25°C
Aspergillus nidulans
2.77
-
NADP+
pH 8.8, 25°C, with shikimate
Toxoplasma gondii
2.78
-
shikimate
pH 8.8, 25°C, with NADP+
Toxoplasma gondii
5.9
-
NADP+
pH 7.0, 25°C, with shikimate
Mycobacterium tuberculosis
7.1
-
NADP+
with shikimate, pH 8.0, 25°C
Helicobacter pylori
7.7
-
shikimate
with NADP+, pH 8.0, 25°C
Helicobacter pylori
8.2
-
shikimate
pH 7.0, 25°C, with NADP+
Mycobacterium tuberculosis
22.8
-
NADP+
pH 7.0, 25°C, with shikimate
Staphylococcus epidermidis
22.8
-
shikimate
pH 7.0, 25°C, with NADP+
Staphylococcus epidermidis
45
-
NADPH
pH 7.0, 25°C, with 3-dehydroshikimate
Mycobacterium tuberculosis
49
-
3-dehydroshikimate
pH 7.0, 25°C, with NADPH
Mycobacterium tuberculosis
55.5
-
NADP+
with shikimate, pH 9.0, 25°C
Aquifex aeolicus
55.5
-
shikimate
with NADP+, pH 9.0, 25°C
Aquifex aeolicus
118
-
3-dehydroshikimate
with NADPH, pH 8.6, 30°C
Corynebacterium glutamicum
135.8
-
shikimate
pH not specified in the publication, 25°C, with NADP+
Staphylococcus aureus
146.2
-
NADP+
pH not specified in the publication, 25°C, with shikimate
Staphylococcus aureus
234
-
shikimate
with NADP+, pH 9.0, 30°C
Corynebacterium glutamicum
237
-
NADP+
with shikimate, pH 9.0, 20°C
Escherichia coli
237
-
shikimate
with NADP+, pH 9.0, 20°C
Escherichia coli
302
-
NADP+
pH 8.8, 25°C, with shikimate
Pseudomonas putida
307
-
shikimate
pH 8.8, 25°C, with NADP+
Pseudomonas putida
390
-
NADP+
with shikimate, pH 7.3, 87°C
Archaeoglobus fulgidus
399
-
NADP+
pH 8.8, 22°C, with shikimate
Arabidopsis thaliana
399
-
NADP+
pH 9.0, 25°C, with shikimate
Mycobacterium tuberculosis
399
-
shikimate
pH 9.0, 25°C, with NADP+
Mycobacterium tuberculosis
428
-
shikimate
pH 8.8, 22°C, with NADP+
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
9
assay at
Mycobacterium tuberculosis
7
-
assay at
Aspergillus nidulans
7.3
-
assay at
Archaeoglobus fulgidus
8
-
assay at
Staphylococcus epidermidis
8.5
-
assay at
Populus trichocarpa
8.8
-
shikimate oxidation assay at
Arabidopsis thaliana
8.8
-
assay at
Pseudomonas putida
8.8
-
assay at
Toxoplasma gondii
9
-
assay at
Aquifex aeolicus
9
-
assay at
Corynebacterium glutamicum
9
-
assay at
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
9
at pH 7.0, the forward reaction catalyzed by Corynebacterium glutamicum SDH proceeds at a rate about 10fold faster than the reverse reaction
Corynebacterium glutamicum
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
cofactor binding might trigger domain movement
Staphylococcus epidermidis
NADP+
dependent on
Aquifex aeolicus
NADP+
dependent on
Archaeoglobus fulgidus
NADP+
dependent on
Aspergillus nidulans
NADP+
dependent on
Corynebacterium glutamicum
NADP+
dependent on
Escherichia coli
NADP+
dependent on
Helicobacter pylori
NADP+
dependent on
Mycobacterium tuberculosis
NADP+
dependent on
Pseudomonas putida
NADP+
dependent on
Staphylococcus aureus
NADP+
dependent on
Staphylococcus epidermidis
NADP+
dependent on
Toxoplasma gondii
NADPH
dependent on
Aquifex aeolicus
NADPH
dependent on
Archaeoglobus fulgidus
NADPH
dependent on
Aspergillus nidulans
NADPH
dependent on
Corynebacterium glutamicum
NADPH
dependent on
Escherichia coli
NADPH
dependent on
Helicobacter pylori
NADPH
dependent on
Mycobacterium tuberculosis
NADPH
dependent on
Pseudomonas putida
NADPH
dependent on
Staphylococcus aureus
NADPH
dependent on
Staphylococcus epidermidis
NADPH
dependent on
Toxoplasma gondii
Application (protein specific)
Application
Commentary
Organism
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Aquifex aeolicus
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Archaeoglobus fulgidus
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Aspergillus nidulans
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Corynebacterium glutamicum
drug development
the essential enzyme is a potential target for antimicrobials
Escherichia coli
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Helicobacter pylori
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Mycobacterium tuberculosis
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Pseudomonas putida
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Staphylococcus aureus
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Staphylococcus epidermidis
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
Toxoplasma gondii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene aroE, recombinant expression
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
cofactor binding might trigger domain movement
Staphylococcus epidermidis
NADP+
dependent on
Aquifex aeolicus
NADP+
dependent on
Archaeoglobus fulgidus
NADP+
dependent on
Aspergillus nidulans
NADP+
dependent on
Corynebacterium glutamicum
NADP+
dependent on
Escherichia coli
NADP+
dependent on
Helicobacter pylori
NADP+
dependent on
Mycobacterium tuberculosis
NADP+
dependent on
Pseudomonas putida
NADP+
dependent on
Staphylococcus aureus
NADP+
dependent on
Staphylococcus epidermidis
NADP+
dependent on
Toxoplasma gondii
NADPH
dependent on
Aquifex aeolicus
NADPH
dependent on
Archaeoglobus fulgidus
NADPH
dependent on
Aspergillus nidulans
NADPH
dependent on
Corynebacterium glutamicum
NADPH
dependent on
Escherichia coli
NADPH
dependent on
Helicobacter pylori
NADPH
dependent on
Mycobacterium tuberculosis
NADPH
dependent on
Pseudomonas putida
NADPH
dependent on
Staphylococcus aureus
NADPH
dependent on
Staphylococcus epidermidis
NADPH
dependent on
Toxoplasma gondii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates
Arabidopsis thaliana
crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO
Staphylococcus epidermidis
crystal structure determination of the apoenzyme, PDB ID 4OMU
Pseudomonas putida
determination of diverse crystal structures with apoenzyme, or enzyme in binary or ternary complexes
Helicobacter pylori
Engineering (protein specific)
Protein Variants
Commentary
Organism
additional information
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
Staphylococcus epidermidis
Q237A
site-directed mutagenesis
Helicobacter pylori
Q237K
site-directed mutagenesis
Helicobacter pylori
Q237N
site-directed mutagenesis
Helicobacter pylori
Y210A
site-directed mutagenesis
Helicobacter pylori
Y210S
site-directed mutagenesis
Helicobacter pylori
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
curcumin
a noncompetitive inhibitor
Helicobacter pylori
additional information
inhibitor screening
Helicobacter pylori
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0091
-
NADP+
pH 8.8, 25°C, with shikimate
Toxoplasma gondii
0.0135
-
NADP+
with shikimate, pH 7.0, 25°C
Aspergillus nidulans
0.022
-
NADP+
pH 7.0, 25°C, with shikimate
Mycobacterium tuberculosis
0.03
-
shikimate
pH 9.0, 25°C, with NADP+
Mycobacterium tuberculosis
0.031
-
3-dehydroshikimate
pH 7.0, 25°C, with NADPH
Mycobacterium tuberculosis
0.031
-
NADPH
pH 7.0, 25°C, with 3-dehydroshikimate
Mycobacterium tuberculosis
0.0375
-
shikimate
pH not specified in the publication, 25°C, with NADP+
Staphylococcus aureus
0.0424
-
NADP+
with shikimate, pH 9.0, 25°C
Aquifex aeolicus
0.0425
-
shikimate
with NADP+, pH 9.0, 25°C
Aquifex aeolicus
0.0426
-
NADP+
pH not specified in the publication, 25°C, with shikimate
Staphylococcus aureus
0.0502
-
shikimate
pH 7.0, 25°C, with NADP+
Mycobacterium tuberculosis
0.0527
-
shikimate
pH 8.8, 25°C, with NADP+
Toxoplasma gondii
0.055
-
NADP+
pH 8.8, 25°C, with shikimate
Pseudomonas putida
0.056
-
NADP+
with shikimate, pH 9.0, 20°C
Escherichia coli
0.063
-
NADP+
pH 9.0, 25°C, with shikimate
Mycobacterium tuberculosis
0.065
-
shikimate
with NADP+, pH 9.0, 20°C
Escherichia coli
0.073
-
shikimate
pH 7.0, 25°C, with NADP+
Staphylococcus epidermidis
0.1
-
NADP+
pH 7.0, 25°C, with shikimate
Staphylococcus epidermidis
0.131
-
NADP+
pH 8.8, 22°C, with shikimate
Arabidopsis thaliana
0.14
-
shikimate
with NADP+, pH 9.0, 30°C
Corynebacterium glutamicum
0.148
-
shikimate
with NADP+, pH 8.0, 25°C
Helicobacter pylori
0.17
-
shikimate
with NADP+, pH 7.3, 87°C
Archaeoglobus fulgidus
0.178
-
shikimate
pH 8.8, 25°C, with NADP+
Pseudomonas putida
0.182
-
NADP+
with shikimate, pH 8.0, 25°C
Helicobacter pylori
0.19
-
NADP+
with shikimate, pH 7.3, 87°C
Archaeoglobus fulgidus
0.223
-
shikimate
pH 8.5, 22°C, with NADP+, isozyme Poptr1
Populus trichocarpa
0.272
-
3-dehydroshikimate
with NADPH, pH 8.6, 30°C
Corynebacterium glutamicum
0.311
-
shikimate
with NADP+, pH 7.0, 25°C
Aspergillus nidulans
0.346
-
shikimate
pH 8.5, 22°C, with NADP+, isozyme Poptr5
Populus trichocarpa
0.685
-
shikimate
pH 8.8, 22°C, with NADP+
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3-dehydroshikimate + NADPH
Populus trichocarpa
-
shikimate + NADP+
-
-
r
3-dehydroshikimate + NADPH
Arabidopsis thaliana
-
shikimate + NADP+
-
-
r
shikimate + NADP+
Staphylococcus aureus
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Escherichia coli
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Helicobacter pylori
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Aquifex aeolicus
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Aspergillus nidulans
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Archaeoglobus fulgidus
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Corynebacterium glutamicum
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Mycobacterium tuberculosis
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Staphylococcus epidermidis
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Toxoplasma gondii
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Archaeoglobus fulgidus ATCC 49558
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Aspergillus nidulans FGSC A4
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Staphylococcus epidermidis ATCC 35984
-
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida KT 2240
-
3-dehydroshikimate + NADPH + H+
-
-
r
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
732
-
pH 7.3, 87°C
Archaeoglobus fulgidus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3-dehydroshikimate + NADPH
-
739956
Populus trichocarpa
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH
-
739956
Arabidopsis thaliana
shikimate + NADP+
-
-
-
r
additional information
no activity with quinate
739956
Helicobacter pylori
?
-
-
-
-
additional information
no activity with quinate
739956
Pseudomonas putida
?
-
-
-
-
additional information
no activity with quinate
739956
Archaeoglobus fulgidus
?
-
-
-
-
additional information
no activity with quinate
739956
Staphylococcus epidermidis
?
-
-
-
-
additional information
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
739956
Populus trichocarpa
?
-
-
-
-
additional information
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
739956
Arabidopsis thaliana
?
-
-
-
-
additional information
the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate
739956
Toxoplasma gondii
?
-
-
-
-
additional information
no activity with quinate
739956
Archaeoglobus fulgidus ATCC 49558
?
-
-
-
-
additional information
no activity with quinate
739956
Staphylococcus epidermidis ATCC 35984
?
-
-
-
-
additional information
no activity with quinate
739956
Pseudomonas putida KT 2240
?
-
-
-
-
shikimate + NADP+
-
739956
Staphylococcus aureus
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Escherichia coli
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Helicobacter pylori
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Aquifex aeolicus
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Pseudomonas putida
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Aspergillus nidulans
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Archaeoglobus fulgidus
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Corynebacterium glutamicum
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Mycobacterium tuberculosis
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Staphylococcus epidermidis
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Toxoplasma gondii
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Archaeoglobus fulgidus ATCC 49558
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Aspergillus nidulans FGSC A4
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Staphylococcus epidermidis ATCC 35984
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
-
739956
Pseudomonas putida KT 2240
3-dehydroshikimate + NADPH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Corynebacterium glutamicum
dimer
-
Mycobacterium tuberculosis
monomer
in solution
Arabidopsis thaliana
monomer
-
Escherichia coli
monomer
-
Staphylococcus epidermidis
More
SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring
Aquifex aeolicus
More
the SDH domain is connected via its N-terminus to the DHQ module
Arabidopsis thaliana
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Escherichia coli
22
-
shikimate oxidation assay at room temperature
Arabidopsis thaliana
22
-
assay at room temperature
Populus trichocarpa
25
-
assay at
Aquifex aeolicus
25
-
assay at
Aspergillus nidulans
25
-
assay at
Mycobacterium tuberculosis
25
-
assay at
Pseudomonas putida
25
-
assay at
Staphylococcus aureus
25
-
assay at
Staphylococcus epidermidis
25
-
assay at
Toxoplasma gondii
30
-
assay at
Corynebacterium glutamicum
87
-
assay at
Archaeoglobus fulgidus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.5
-
shikimate
with NADP+, pH 7.0, 25°C
Aspergillus nidulans
2.77
-
NADP+
pH 8.8, 25°C, with shikimate
Toxoplasma gondii
2.78
-
shikimate
pH 8.8, 25°C, with NADP+
Toxoplasma gondii
5.9
-
NADP+
pH 7.0, 25°C, with shikimate
Mycobacterium tuberculosis
7.1
-
NADP+
with shikimate, pH 8.0, 25°C
Helicobacter pylori
7.7
-
shikimate
with NADP+, pH 8.0, 25°C
Helicobacter pylori
8.2
-
shikimate
pH 7.0, 25°C, with NADP+
Mycobacterium tuberculosis
22.8
-
NADP+
pH 7.0, 25°C, with shikimate
Staphylococcus epidermidis
22.8
-
shikimate
pH 7.0, 25°C, with NADP+
Staphylococcus epidermidis
45
-
NADPH
pH 7.0, 25°C, with 3-dehydroshikimate
Mycobacterium tuberculosis
49
-
3-dehydroshikimate
pH 7.0, 25°C, with NADPH
Mycobacterium tuberculosis
55.5
-
NADP+
with shikimate, pH 9.0, 25°C
Aquifex aeolicus
55.5
-
shikimate
with NADP+, pH 9.0, 25°C
Aquifex aeolicus
118
-
3-dehydroshikimate
with NADPH, pH 8.6, 30°C
Corynebacterium glutamicum
135.8
-
shikimate
pH not specified in the publication, 25°C, with NADP+
Staphylococcus aureus
146.2
-
NADP+
pH not specified in the publication, 25°C, with shikimate
Staphylococcus aureus
234
-
shikimate
with NADP+, pH 9.0, 30°C
Corynebacterium glutamicum
237
-
NADP+
with shikimate, pH 9.0, 20°C
Escherichia coli
237
-
shikimate
with NADP+, pH 9.0, 20°C
Escherichia coli
302
-
NADP+
pH 8.8, 25°C, with shikimate
Pseudomonas putida
307
-
shikimate
pH 8.8, 25°C, with NADP+
Pseudomonas putida
390
-
NADP+
with shikimate, pH 7.3, 87°C
Archaeoglobus fulgidus
399
-
NADP+
pH 8.8, 22°C, with shikimate
Arabidopsis thaliana
399
-
NADP+
pH 9.0, 25°C, with shikimate
Mycobacterium tuberculosis
399
-
shikimate
pH 9.0, 25°C, with NADP+
Mycobacterium tuberculosis
428
-
shikimate
pH 8.8, 22°C, with NADP+
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
9
assay at
Mycobacterium tuberculosis
7
-
assay at
Aspergillus nidulans
7.3
-
assay at
Archaeoglobus fulgidus
8
-
assay at
Staphylococcus epidermidis
8.5
-
assay at
Populus trichocarpa
8.8
-
shikimate oxidation assay at
Arabidopsis thaliana
8.8
-
assay at
Pseudomonas putida
8.8
-
assay at
Toxoplasma gondii
9
-
assay at
Aquifex aeolicus
9
-
assay at
Corynebacterium glutamicum
9
-
assay at
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
9
at pH 7.0, the forward reaction catalyzed by Corynebacterium glutamicum SDH proceeds at a rate about 10fold faster than the reverse reaction
Corynebacterium glutamicum
General Information
General Information
Commentary
Organism
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Aquifex aeolicus
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Archaeoglobus fulgidus
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Aspergillus nidulans
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Corynebacterium glutamicum
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Escherichia coli
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Helicobacter pylori
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Mycobacterium tuberculosis
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Pseudomonas putida
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Staphylococcus aureus
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Staphylococcus epidermidis
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Toxoplasma gondii
malfunction
a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate
Arabidopsis thaliana
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Aquifex aeolicus
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway, (B) the quinate pathway, (C) the aminoshikimate pathway, overview
Arabidopsis thaliana
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Archaeoglobus fulgidus
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
Aspergillus nidulans
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Corynebacterium glutamicum
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Escherichia coli
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Helicobacter pylori
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Mycobacterium tuberculosis
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway. (B) the quinate pathway. (C) the aminoshikimate pathway, overview
Populus trichocarpa
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Pseudomonas putida
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Staphylococcus aureus
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Staphylococcus epidermidis
metabolism
the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Toxoplasma gondii
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ-SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ-SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processe. Crystallization of the Arabidopsis thaliana protein with shikimate bound in the SDH domain and tartrate (a component of the crystallization solution) in the DHQ domain reveals a V-shaped orientation of the domains. Addition of NADP+ to DHQ–SDH crystals already containing shikimate in the SDH domain results in the production of 3-dehydroshikimate by the SDH domain and the transfer of the compound to the DHQ active sites
Arabidopsis thaliana
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ–SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ–SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes
Populus trichocarpa
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes, the enzyme reaction represents the fourth step of the shikimate pathway
Aquifex aeolicus
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Archaeoglobus fulgidus
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Aspergillus nidulans
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Corynebacterium glutamicum
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Escherichia coli
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Helicobacter pylori
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Mycobacterium tuberculosis
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Pseudomonas putida
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Staphylococcus aureus
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Staphylococcus epidermidis
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Toxoplasma gondii
General Information (protein specific)
General Information
Commentary
Organism
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Aquifex aeolicus
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Archaeoglobus fulgidus
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Aspergillus nidulans
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Corynebacterium glutamicum
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Escherichia coli
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Helicobacter pylori
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Mycobacterium tuberculosis
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Pseudomonas putida
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Staphylococcus aureus
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Staphylococcus epidermidis
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
Toxoplasma gondii
malfunction
a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate
Arabidopsis thaliana
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Aquifex aeolicus
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway, (B) the quinate pathway, (C) the aminoshikimate pathway, overview
Arabidopsis thaliana
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Archaeoglobus fulgidus
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
Aspergillus nidulans
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Corynebacterium glutamicum
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Escherichia coli
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Helicobacter pylori
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Mycobacterium tuberculosis
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway. (B) the quinate pathway. (C) the aminoshikimate pathway, overview
Populus trichocarpa
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Pseudomonas putida
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Staphylococcus aureus
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Staphylococcus epidermidis
metabolism
the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
Toxoplasma gondii
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ-SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ-SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processe. Crystallization of the Arabidopsis thaliana protein with shikimate bound in the SDH domain and tartrate (a component of the crystallization solution) in the DHQ domain reveals a V-shaped orientation of the domains. Addition of NADP+ to DHQ–SDH crystals already containing shikimate in the SDH domain results in the production of 3-dehydroshikimate by the SDH domain and the transfer of the compound to the DHQ active sites
Arabidopsis thaliana
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ–SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ–SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes
Populus trichocarpa
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes, the enzyme reaction represents the fourth step of the shikimate pathway
Aquifex aeolicus
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Archaeoglobus fulgidus
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Aspergillus nidulans
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Corynebacterium glutamicum
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Escherichia coli
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Helicobacter pylori
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Mycobacterium tuberculosis
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Pseudomonas putida
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Staphylococcus aureus
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Staphylococcus epidermidis
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
Toxoplasma gondii
Other publictions for EC 1.1.1.25
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
Synonyms
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)
740821
Bontpart
Two shikimate dehydrogenases, ...
Vitis vinifera
J. Exp. Bot.
67
3537-3550
2016
-
-
1
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-
13
1
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4
-
5
-
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4
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8
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8
1
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12
2
-
-
2
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4
8
-
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13
1
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4
-
-
-
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-
15
-
-
8
-
4
-
-
12
7
-
-
-
-
2
8
-
12
12
739956
Peek
The shikimate dehydrogenase fa ...
Aquifex aeolicus, Arabidopsis thaliana, Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558, Aspergillus nidulans, Aspergillus nidulans FGSC A4, Corynebacterium glutamicum, Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Populus trichocarpa, Pseudomonas putida, Pseudomonas putida KT 2240, Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus epidermidis ATCC 35984, Toxoplasma gondii
Arch. Biochem. Biophys.
566
85-99
2015
-
11
1
4
6
-
2
30
-
-
-
17
-
19
-
-
-
-
-
-
1
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27
7
19
12
-
-
26
11
1
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23
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11
1
23
4
6
-
-
2
-
30
-
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-
17
-
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-
1
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27
7
12
-
-
26
11
1
-
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-
38
38
-
-
-
740347
Prus-Glowacki
-
Shikimate dehydrogenase (E.C. ...
Pinus sylvestris
Dendrobiology
73
153-162
2015
-
1
1
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-
-
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1
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741401
Li
-
SAR studies on 1,2,4-triazolo[ ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
RSC Adv.
5
97089-97101
2015
-
1
-
-
-
-
26
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-
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2
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2
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2
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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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1
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26
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2
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2
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1
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1
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-
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-
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-
-
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-
741411
Zhang
Determination of the cytosolic ...
Escherichia coli
Sci. Rep.
5
12846
2015
-
1
1
-
1
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2
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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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2
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2
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1
1
2
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1
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2
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1
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2
-
2
-
2
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-
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2
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-
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-
1
1
-
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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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-
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5
1
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7
-
5
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1
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-
5
-
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15
1
4
1
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1
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5
-
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-
1
5
-
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5
1
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7
-
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1
-
5
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15
1
1
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-
1
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-
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-
4
4
-
-
-
740771
Peek
Identification of novel polyph ...
Arabidopsis thaliana, Pseudomonas putida, Pseudomonas putida KT 2240
J. Biomol. Screen.
19
1090-1098
2014
-
-
2
1
-
-
27
-
-
-
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3
-
9
-
-
2
-
-
-
-
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4
-
6
2
-
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2
-
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4
-
-
4
-
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2
4
1
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4
27
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3
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2
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4
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2
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2
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-
-
-
-
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740978
Peek
Isolation and molecular charac ...
Toxoplasma gondii
Mol. Biochem. Parasitol.
194
16-19
2014
-
-
-
-
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2
2
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1
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3
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1
2
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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1
2
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2
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1
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1
2
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-
1
1
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-
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3
3
-
-
-
741030
Avitia-Dominguez
Inhibition and biochemical cha ...
Staphylococcus aureus, Staphylococcus aureus ATCC MRSA252
Molecules
19
4491-4509
2014
-
1
1
-
-
-
10
3
-
-
1
2
-
6
-
-
1
1
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-
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2
2
3
1
1
-
2
1
1
-
1
1
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1
1
1
-
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-
-
10
1
3
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1
2
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1
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-
2
2
1
1
-
2
1
1
-
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-
-
-
-
2
2
724089
Kubota
Characterization of shikimate ...
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
Appl. Microbiol. Biotechnol.
97
8139-8149
2013
-
-
1
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2
6
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1
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5
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12
1
5
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6
4
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5
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2
6
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4
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6
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2
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12
2
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6
4
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-
1
1
1
1
6
6
725977
Lee
High-resolution structure of s ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Mol. Cells
33
229-233
2012
-
-
-
1
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-
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4
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1
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721203
Lee
Overexpression, crystallizatio ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558
Acta Crystallogr. Sect. F
67
1556-1558
2011
-
1
1
1
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-
-
-
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2
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5
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1
5
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1
1
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1
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2
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1
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723859
Lee
Overexpression, crystallizatio ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Acta Crystallogr. Sect. F
67
824-826
2011
-
-
1
1
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2
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5
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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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-
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-
704148
Cao
Effect of BTH on anthocyanin c ...
Fragaria x ananassa
J. Agric. Food Chem.
58
5801-5805
2010
2
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-
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1
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2
3
2
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2
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2
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1
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2
3
2
2
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2
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1
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1
1
-
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-
697894
Han
X-ray crystallographic and enz ...
Staphylococcus epidermidis RP62A
FEBS J.
276
1125-1139
2009
-
-
1
1
1
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5
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2
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2
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1
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2
1
1
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3
1
1
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1
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1
1
1
1
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5
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2
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1
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2
1
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3
1
1
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-
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698320
Rodrigues
Homogeneous recombinant Mycoba ...
Mycobacterium tuberculosis
Int. J. Biol. Macromol.
45
200-205
2009
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1
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6
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2
1
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1
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2
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1
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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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6
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2
1
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1
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1
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2
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1
1
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1
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-
-
-
-
-
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-
699631
Barcellos
Structural studies of shikimat ...
Bacillus anthracis
J. Mol. Model.
15
147-155
2009
-
-
-
-
-
-
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1
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4
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1
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1
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711616
Rodrigues
The conserved Lysine69 residue ...
Mycobacterium tuberculosis, no activity in Homo sapiens
BMC Res. Notes
2
227
2009
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1
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1
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5
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1
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4
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1
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2
1
1
1
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2
1
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2
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1
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1
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5
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1
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2
1
1
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2
1
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-
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2
2
-
4
4
684153
Schoepe
1.6 A structure of an NAD(+)-d ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
803-809
2008
-
-
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1
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2
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1
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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
1
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2
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2
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2
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-
689956
Arcuri
Structural studies of shikimat ...
Mycobacterium tuberculosis
Proteins
72
720-730
2008
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-
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1
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7
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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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694093
Singh
A phylogenomic analysis of the ...
Pseudomonas putida, Pseudomonas putida KT 2240, Pseudomonas putida KT2440
Mol. Biol. Evol.
25
2221-2232
2008
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-
2
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17
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12
-
15
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2
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2
18
-
18
1
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23
1
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3
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7
7
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18
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12
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7
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2
18
-
4
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26
4
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681134
Ding
Functional analysis of the ess ...
Nicotiana tabacum
J. Exp. Bot.
58
2053-2067
2007
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1
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1
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2
3
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6
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3
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1
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1
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11
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6
2
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3
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2
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3
4
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3
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4
3
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6
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2
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2
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11
-
4
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4
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-
684670
Fonseca
Kinetic and chemical mechanism ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Arch. Biochem. Biophys.
457
123-133
2007
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-
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2
2
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4
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1
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1
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1
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685190
Gan
Structural and biochemical ana ...
Aquifex aeolicus
Biochemistry
46
9513-9522
2007
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1
1
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2
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3
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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
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-
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-
686243
Singh
-
The DHQ-dehydroshikimate-SDH-s ...
Arabidopsis thaliana
Cryst. Growth Des.
7
2153-2160
2007
-
-
1
1
8
-
-
16
-
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1
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1
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1
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16
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1
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1
8
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16
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1
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16
-
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-
-
-
-
-
-
688379
Bagautdinov
Crystal structures of shikimat ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Mol. Biol.
373
424-438
2007
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1
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5
-
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1
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-
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-
667097
Schoepe
Cloning, expression, purificat ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
F62
635-637
2006
-
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1
1
-
-
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3
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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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-
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-
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-
-
667700
Singh
Structure of Arabidopsis dehyd ...
Arabidopsis thaliana
Biochemistry
45
10406
2006
-
-
1
1
10
-
-
18
-
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2
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1
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1
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1
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3
-
4
1
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18
1
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2
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1
2
1
10
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18
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2
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1
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
-
-
668019
Adachi
Purification and properties of ...
Gluconobacter oxydans, Gluconobacter oxydans IFO 3244
Biosci. Biotechnol. Biochem.
70
2786-2789
2006
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-
-
-
-
-
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2
2
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6
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1
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2
2
2
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2
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2
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2
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2
2
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1
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-
2
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
668576
Han
Biochemical characterization a ...
Helicobacter pylori, Helicobacter pylori SS1
FEBS J.
273
4682-4692
2006
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1
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6
3
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2
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4
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1
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1
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6
1
1
1
1
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3
1
1
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4
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5
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1
4
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5
6
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3
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2
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1
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1
-
6
1
1
1
-
3
1
1
-
-
-
-
-
-
-
-
670786
Fonseca
Functional shikimate dehydroge ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
46
429-437
2006
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1
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5
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5
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7
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1
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1
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1
2
2
1
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2
4
1
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1
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1
1
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5
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5
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1
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1
-
1
2
1
-
2
4
1
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-
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669163
Zhang
Expression, purification and p ...
Mycobacterium tuberculosis
J. Biochem. Mol. Biol.
38
624-631
2005
2
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1
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1
1
3
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1
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4
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1
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1
2
1
1
2
1
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1
2
1
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2
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2
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1
2
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1
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1
-
3
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1
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1
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1
2
1
1
1
-
1
2
1
-
-
-
-
-
-
-
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669328
Singh
Crystal structure of a novel s ...
Haemophilus influenzae
J. Biol. Chem.
280
17101-17108
2005
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1
1
2
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1
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1
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2
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2
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1
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-
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2
1
2
1
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2
1
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2
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1
2
1
2
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1
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1
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2
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2
1
1
-
-
-
2
1
-
-
-
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-
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-
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655639
Lim
A thermostable shikimate 5-deh ...
Archaeoglobus fulgidus
FEMS Microbiol. Lett.
238
101-106
2004
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1
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3
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3
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4
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2
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2
1
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2
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3
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1
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2
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1
2
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3
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-
3
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-
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-
2
-
2
1
2
-
3
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-
1
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-
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655854
Ye
The crystal structure of shiki ...
Haemophilus influenzae
J. Bacteriol.
185
4144-4151
2003
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1
1
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3
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2
1
1
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2
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1
2
2
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1
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-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657359
Padyana
Crystal structure of shikimate ...
Methanocaldococcus jannaschii
Structure
11
1005-1013
2003
-
-
1
1
-
-
-
-
-
-
2
1
-
4
-
-
1
-
-
-
-
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1
2
2
-
-
-
-
-
-
-
2
-
-
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-
-
1
2
1
-
-
-
-
-
-
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2
1
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-
-
1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670901
Vogan
Shikimate dehydrogenase struct ...
Methanocaldococcus jannaschii
Structure
11
902-903
2003
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
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1
1
2
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-
-
-
-
-
-
1
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-
-
-
1
-
-
-
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-
-
-
1
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-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657254
Magalhaes
Cloning and expression of func ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
26
59-64
2002
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1
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-
-
-
-
-
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1
-
-
180
-
-
1
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286396
Maclean
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. D
56
512-515
2000
-
-
1
1
-
-
-
-
-
-
3
1
-
2
-
-
1
-
-
-
-
1
1
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
-
-
3
1
-
-
-
1
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286398
Diaz
-
Shikimate dehydrogenase from p ...
Capsicum annuum
Physiol. Plant.
100
147-152
1997
4
-
-
-
-
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5
2
-
-
1
2
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1
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1
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-
-
-
-
2
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1
-
1
-
1
1
1
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-
-
-
4
-
-
-
-
-
-
-
5
-
2
-
-
1
2
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-
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1
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-
-
-
2
-
1
-
1
-
1
1
1
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286397
Lourenco
-
Purification and properties of ...
Cucumis sativus
J. Agric. Food Chem.
39
458-462
1991
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1
5
2
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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
-
-
1
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
2
-
-
1
1
-
-
-
1
-
-
2
-
1
-
1
1
1
-
1
-
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-
286386
Chaudhuri
The purification of shikimate ...
Escherichia coli
Biochem. J.
226
217-223
1985
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1
1
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1
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1
1
1
1
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-
-
-
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-
2
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-
-
-
-
-
2
-
-
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-
-
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-
1
1
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-
-
1
-
-
1
1
1
1
-
-
-
-
-
-
-
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-
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-
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286394
Lemos Silva
-
Inhibition of shikimate dehydr ...
Euterpe oleracea
J. Food Biochem.
9
105-116
1985
-
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7
1
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1
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-
-
1
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-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
7
-
1
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1
1
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-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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286387
Lourenco
-
Partial purification and some ...
Solanum lycopersicum
Phytochemistry
23
497-499
1984
-
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-
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8
2
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1
1
1
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1
-
-
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1
1
-
1
-
-
-
-
1
-
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
8
-
2
-
1
1
1
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-
-
-
-
1
1
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
5466
Polley
Purification and characterizat ...
Physcomitrella patens
Biochim. Biophys. Acta
526
259-266
1978
-
-
-
-
-
-
-
-
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1
1
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3
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1
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-
-
-
-
1
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
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-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
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286388
Koshiba
Purification of two forms of t ...
Vigna mungo
Biochim. Biophys. Acta
522
10-18
1978
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-
-
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4
3
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1
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1
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2
1
-
1
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-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
3
-
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1
1
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1
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2
1
-
1
-
1
-
-
-
1
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-
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5464
Jacobson
Purification and stability of ...
Neurospora crassa
Biochim. Biophys. Acta
289
1-12
1972
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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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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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-
-
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286390
Higuchi
-
Changes in activity of shikima ...
Bambusa sp.
Plant Cell Physiol.
8
61-69
1967
-
-
-
-
-
-
-
-
-
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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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286389
Sanderson
5-Dehydroshikimate reductase i ...
Camellia sinensis
Biochem. J.
98
248-252
1966
-
-
-
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3
2
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1
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-
-
1
-
-
1
-
-
1
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
2
-
-
-
1
-
-
-
-
-
1
-
-
1
-
1
-
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