BRENDA - Enzyme Database show
show all sequences of 1.1.1.25

Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway

Singh, S.A.; Christendat, D.; Biochemistry 45, 10406 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Arabidopsis thaliana
Crystallization (Commentary)
Crystallization
Organism
purified native and selenomethionine-labeled DELTA88DHQ-SDH complexed with shikimate, hanging drop vapour diffusion method, 10 mg/ml protein in 1 mM shikimate mixed with equal volume of reservoir solution containing 0.4 M potassium sodium tartrate tetrahydrate, 0.1 M tri-sodium dihydrate, pH 5.6, and 2.8 M ammonium sulfate, X-ray diffraction structure determination and analysi at 1.95-2.2 A resolution
Arabidopsis thaliana
Engineering
Amino acid exchange
Commentary
Organism
D423A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, inactive mutant
Arabidopsis thaliana
D423N
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
K385A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
K385N
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
K385N/D423N
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
additional information
construction of deletion variant DELTA88DHQ-SDH, thermal denaturation analysis, overview
Arabidopsis thaliana
S336A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
S338A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
Y550A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
Y550F
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
NADP+
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.022
-
NADP+
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.053
-
NADP+
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.079
-
NADP+
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
0.114
-
NADP+
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
0.131
-
NADP+
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
0.131
-
shikimate
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.132
-
NADP+
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
0.152
-
NADP+
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
0.157
-
NADP+
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
0.263
-
shikimate
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.47
-
shikimate
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.555
-
shikimate
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
0.685
-
shikimate
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
1.03
-
shikimate
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
1.06
-
shikimate
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
6.2
-
shikimate
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
8.74
-
shikimate
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroshikimate + NADPH
Arabidopsis thaliana
-
shikimate + NADP+
-
-
r
additional information
Arabidopsis thaliana
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
-
bifunctional enzyme
-
Reaction
Reaction
Commentary
Organism
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
active site structure, reaction and kinetic mechanisms
Arabidopsis thaliana
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroshikimate + NADPH
-
667700
Arabidopsis thaliana
shikimate + NADP+
-
-
-
r
additional information
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
667700
Arabidopsis thaliana
?
-
-
-
-
additional information
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities
667700
Arabidopsis thaliana
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Arabidopsis thaliana
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.008
-
NADP+
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.013
-
shikimate
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.036
-
NADP+
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.043
-
shikimate
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.063
-
shikimate
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.066
-
NADP+
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.092
-
NADP+
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
0.121
-
shikimate
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
1.86
-
NADP+
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
2.1
-
shikimate
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
3.11
-
NADP+
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
3.9
-
shikimate
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
11.2
-
NADP+
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
33.2
-
shikimate
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
52.9
-
NADP+
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
140
-
shikimate
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
399
-
NADP+
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
428
-
shikimate
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Arabidopsis thaliana
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Arabidopsis thaliana
NADPH
-
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Arabidopsis thaliana
NADPH
-
Arabidopsis thaliana
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified native and selenomethionine-labeled DELTA88DHQ-SDH complexed with shikimate, hanging drop vapour diffusion method, 10 mg/ml protein in 1 mM shikimate mixed with equal volume of reservoir solution containing 0.4 M potassium sodium tartrate tetrahydrate, 0.1 M tri-sodium dihydrate, pH 5.6, and 2.8 M ammonium sulfate, X-ray diffraction structure determination and analysi at 1.95-2.2 A resolution
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D423A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, inactive mutant
Arabidopsis thaliana
D423N
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
K385A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
K385N
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
K385N/D423N
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
additional information
construction of deletion variant DELTA88DHQ-SDH, thermal denaturation analysis, overview
Arabidopsis thaliana
S336A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
S338A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
Y550A
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
Y550F
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Arabidopsis thaliana
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.017
-
NADP+
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.022
-
NADP+
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.053
-
NADP+
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.079
-
NADP+
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
0.114
-
NADP+
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
0.131
-
NADP+
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
0.131
-
shikimate
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.132
-
NADP+
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
0.152
-
NADP+
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
0.157
-
NADP+
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
0.263
-
shikimate
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.47
-
shikimate
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.555
-
shikimate
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
0.685
-
shikimate
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
1.03
-
shikimate
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
1.06
-
shikimate
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
6.2
-
shikimate
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
8.74
-
shikimate
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroshikimate + NADPH
Arabidopsis thaliana
-
shikimate + NADP+
-
-
r
additional information
Arabidopsis thaliana
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
?
-
-
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroshikimate + NADPH
-
667700
Arabidopsis thaliana
shikimate + NADP+
-
-
-
r
additional information
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
667700
Arabidopsis thaliana
?
-
-
-
-
additional information
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities
667700
Arabidopsis thaliana
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Arabidopsis thaliana
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.008
-
NADP+
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.013
-
shikimate
pH 7.5, 22°C, mutant K385A
Arabidopsis thaliana
0.036
-
NADP+
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.043
-
shikimate
pH 7.5, 22°C, mutant K385N/D423N
Arabidopsis thaliana
0.063
-
shikimate
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.066
-
NADP+
pH 7.5, 22°C, mutant K385N
Arabidopsis thaliana
0.092
-
NADP+
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
0.121
-
shikimate
pH 7.5, 22°C, mutant D423N
Arabidopsis thaliana
1.86
-
NADP+
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
2.1
-
shikimate
pH 7.5, 22°C, mutant Y550A
Arabidopsis thaliana
3.11
-
NADP+
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
3.9
-
shikimate
pH 7.5, 22°C, mutant Y550F
Arabidopsis thaliana
11.2
-
NADP+
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
33.2
-
shikimate
pH 7.5, 22°C, mutant S338A
Arabidopsis thaliana
52.9
-
NADP+
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
140
-
shikimate
pH 7.5, 22°C, mutant S336A
Arabidopsis thaliana
399
-
NADP+
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
428
-
shikimate
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Arabidopsis thaliana
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
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)
724089
Kubota
Characterization of shikimate ...
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
Appl. Microbiol. Biotechnol.
97
8139-8149
2013
-
-
1
-
-
-
2
6
-
-
1
-
-
5
-
-
-
-
-
-
-
-
12
1
-
-
-
6
4
-
-
5
-
-
-
-
-
2
6
-
-
-
-
4
-
6
-
-
2
-
-
-
-
-
-
-
-
-
12
2
-
-
-
6
4
-
-
-
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
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721203
Lee
Overexpression, crystallizatio ...
Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558
Acta Crystallogr. Sect. F
67
1556-1558
2011
-
1
1
1
-
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723859
Lee
Overexpression, crystallizatio ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Acta Crystallogr. Sect. F
67
824-826
2011
-
-
1
1
-
-
-
-
-
-
2
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
704148
Cao
Effect of BTH on anthocyanin c ...
Fragaria x ananassa
J. Agric. Food Chem.
58
5801-5805
2010
2
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
2
3
2
2
-
2
-
-
-
1
-
-
2
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
3
2
2
-
2
-
-
-
1
-
-
-
-
1
1
-
-
-
697894
Han
X-ray crystallographic and enz ...
Staphylococcus epidermidis RP62A
FEBS J.
276
1125-1139
2009
-
-
1
1
1
-
-
5
-
-
2
-
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
3
1
1
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
5
-
-
2
-
-
-
-
1
-
-
-
-
2
1
-
-
-
3
1
1
-
-
-
-
-
-
-
-
698320
Rodrigues
Homogeneous recombinant Mycoba ...
Mycobacterium tuberculosis
Int. J. Biol. Macromol.
45
200-205
2009
-
-
1
-
6
-
-
2
1
-
1
-
-
2
-
-
1
-
-
-
2
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
2
1
-
1
-
-
-
-
1
-
-
2
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
699631
Barcellos
Structural studies of shikimat ...
Bacillus anthracis
J. Mol. Model.
15
147-155
2009
-
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
711616
Rodrigues
The conserved Lysine69 residue ...
Mycobacterium tuberculosis, no activity in Homo sapiens
BMC Res. Notes
2
227
2009
-
1
-
-
1
-
-
5
-
-
-
1
-
4
-
-
-
1
-
-
-
-
2
1
1
-
-
2
1
-
-
2
-
-
-
-
1
-
2
-
1
-
-
-
-
5
-
-
-
1
-
-
-
-
-
-
-
-
2
1
1
-
-
2
1
-
-
-
-
2
2
-
4
4
684153
Schoepe
1.6 A structure of an NAD(+)-d ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
803-809
2008
-
-
-
1
-
-
-
2
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
689956
Arcuri
Structural studies of shikimat ...
Mycobacterium tuberculosis
Proteins
72
720-730
2008
-
-
-
1
-
-
-
-
-
-
-
-
-
7
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
694093
Singh
A phylogenomic analysis of the ...
Pseudomonas putida, Pseudomonas putida KT2240, Pseudomonas putida KT2440
Mol. Biol. Evol.
25
2221-2232
2008
-
-
2
-
-
-
-
16
-
-
-
8
-
8
-
-
2
-
-
-
-
2
14
-
1
-
-
22
1
-
-
3
-
-
-
-
-
7
7
-
-
-
-
-
-
16
-
-
-
8
-
-
-
7
-
-
-
2
14
-
4
-
-
22
4
-
-
-
-
-
-
-
-
-
681134
Ding
Functional analysis of the ess ...
Nicotiana tabacum
J. Exp. Bot.
58
2053-2067
2007
-
-
1
-
1
-
-
2
3
-
-
6
-
3
-
-
1
-
-
1
-
-
11
-
2
-
-
-
3
-
-
2
-
-
-
-
-
3
4
-
3
-
-
-
-
4
3
-
-
6
-
-
-
2
-
2
-
-
11
-
4
-
-
-
4
-
-
-
-
-
-
-
-
-
684670
Fonseca
Kinetic and chemical mechanism ...
Mycobacterium tuberculosis
Arch. Biochem. Biophys.
457
123-133
2007
-
-
-
-
-
-
2
2
-
-
-
-
-
2
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
685190
Gan
Structural and biochemical ana ...
Aquifex aeolicus
Biochemistry
46
9513-9522
2007
-
-
1
1
-
-
-
2
-
-
-
-
-
4
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
686243
Singh
-
The DHQ-dehydroshikimate-SDH-s ...
Arabidopsis thaliana
Cryst. Growth Des.
7
2153-2160
2007
-
-
1
1
8
-
-
16
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
16
-
-
-
-
-
-
-
-
-
1
-
1
8
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
688379
Bagautdinov
Crystal structures of shikimat ...
Thermus thermophilus
J. Mol. Biol.
373
424-438
2007
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667097
Schoepe
Cloning, expression, purificat ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
F62
635-637
2006
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667700
Singh
Structure of Arabidopsis dehyd ...
Arabidopsis thaliana
Biochemistry
45
10406
2006
-
-
1
1
10
-
-
18
-
-
-
2
-
1
-
-
-
1
-
-
1
-
3
-
1
-
-
18
1
-
-
2
-
-
-
-
-
1
2
1
10
-
-
-
-
18
-
-
-
2
-
-
-
-
-
-
1
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
-
-
668019
Adachi
Purification and properties of ...
Gluconobacter oxydans, Gluconobacter oxydans IFO 3244
Biosci. Biotechnol. Biochem.
70
2786-2789
2006
-
-
-
-
-
-
-
-
-
-
2
2
-
6
-
-
-
-
-
1
-
-
2
2
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
1
-
-
2
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
668576
Han
Biochemical characterization a ...
Helicobacter pylori, Helicobacter pylori SS1
FEBS J.
273
4682-4692
2006
-
-
1
-
-
-
6
3
-
-
-
2
-
4
-
-
1
-
-
-
1
-
6
1
1
1
-
3
1
1
-
4
-
-
5
-
-
1
4
-
-
-
5
6
-
3
-
-
-
2
-
-
-
1
-
-
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
-
-
1
-
-
-
-
5
-
-
5
-
-
7
-
-
1
-
-
-
1
-
1
2
1
-
2
4
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
5
-
-
5
-
-
-
-
1
-
-
1
-
1
2
1
-
2
4
1
-
-
-
-
-
-
-
-
-
669163
Zhang
Expression, purification and p ...
Mycobacterium tuberculosis
J. Biochem. Mol. Biol.
38
624-631
2005
2
-
1
-
-
1
1
3
-
-
-
1
-
4
-
-
1
-
-
-
1
2
1
1
1
-
1
2
1
-
-
2
-
-
-
2
-
1
2
-
-
1
-
1
-
3
-
-
-
1
-
-
-
1
-
-
1
2
1
1
1
-
1
2
1
-
-
-
-
-
-
-
-
-
669328
Singh
Crystal structure of a novel s ...
Haemophilus influenzae
J. Biol. Chem.
280
17101-17108
2005
-
-
1
1
2
-
1
-
-
1
-
2
-
2
-
-
-
1
-
-
-
-
2
1
1
-
-
-
2
1
-
2
-
-
-
-
-
1
2
1
2
-
-
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
1
1
-
-
-
2
1
-
-
-
-
-
-
-
-
655639
Lim
A thermostable shikimate 5-deh ...
Archaeoglobus fulgidus
FEMS Microbiol. Lett.
238
101-106
2004
-
-
1
-
-
-
-
3
-
-
3
-
-
4
-
-
-
-
-
-
2
-
2
1
2
-
3
-
-
1
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
2
-
2
1
2
-
3
-
-
1
-
-
-
-
-
-
-
-
655854
Ye
The crystal structure of shiki ...
Haemophilus influenzae
J. Bacteriol.
185
4144-4151
2003
-
-
1
1
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657359
Padyana
Crystal structure of shikimate ...
Methanocaldococcus jannaschii
Structure
11
1005-1013
2003
-
-
1
1
-
-
-
-
-
-
2
1
-
4
-
-
1
-
-
-
-
-
1
2
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670901
Vogan
Shikimate dehydrogenase struct ...
Methanocaldococcus jannaschii
Structure
11
902-903
2003
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657254
Magalhaes
Cloning and expression of func ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
26
59-64
2002
-
-
1
-
-
-
-
-
-
-
1
-
-
145
-
-
1
-
-
-
-
-
-
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
-
-
-
-
-
5
2
-
-
1
2
-
1
-
-
1
-
-
-
-
-
2
-
1
-
1
-
1
1
1
-
-
-
-
4
-
-
-
-
-
-
-
5
-
2
-
-
1
2
-
-
-
1
-
-
-
-
2
-
1
-
1
-
1
1
1
-
-
-
-
-
-
-
286397
Lourenco
Purification and properties of ...
Cucumis sativus
J. Agric. Food Chem.
39
458-462
1991
-
-
-
-
-
1
5
2
-
-
1
1
-
1
-
-
1
-
-
-
2
-
1
-
1
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
2
-
-
1
1
-
-
-
1
-
-
2
-
1
-
1
1
1
-
1
-
-
-
-
-
-
-
-
-
286386
Chaudhuri
The purification of shikimate ...
Escherichia coli
Biochem. J.
226
217-223
1985
-
-
-
-
-
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
1
1
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
1
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286394
Lemos Silva
Inhibition of shikimate dehydr ...
Euterpe oleracea
J. Food Biochem.
9
105-116
1985
-
-
-
-
-
-
7
1
-
-
1
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
1
-
-
1
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286387
Lourenco
-
Partial purification and some ...
Solanum lycopersicum
Phytochemistry
23
497-499
1984
-
-
-
-
-
-
8
2
-
1
1
1
-
1
-
-
-
-
-
1
1
-
1
-
-
-
1
-
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
8
-
2
-
1
1
1
-
-
-
-
-
1
1
-
1
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
5466
Polley
Purification and characterizat ...
Physcomitrella patens
Biochim. Biophys. Acta
526
259-266
1978
-
-
-
-
-
-
-
-
-
-
1
1
-
3
-
-
1
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
286388
Koshiba
Purification of two forms of t ...
Vigna mungo
Biochim. Biophys. Acta
522
10-18
1978
-
-
-
-
-
-
4
3
-
-
1
1
-
2
-
-
1
-
-
2
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
3
-
-
1
1
-
-
-
1
-
2
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
5464
Jacobson
Purification and stability of ...
Neurospora crassa
Biochim. Biophys. Acta
289
1-12
1972
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286390
Higuchi
-
Changes in activity of shikima ...
Bambusa sp.
Plant Cell Physiol.
8
61-69
1967
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286389
Sanderson
5-Dehydroshikimate reductase i ...
Camellia sinensis
Biochem. J.
98
248-252
1966
-
-
-
-
-
-
3
2
-
-
-
1
-
3
-
-
-
-
-
1
-
-
1
-
1
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
2
-
-
-
1
-
-
-
-
-
1
-
-
1
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
286393
Balinsky
Aromatic biosynthesis in highe ...
Pisum sativum
Biochem. J.
80
292-296
1961
-
-
-
-
-
-
2
2
-
1
1
3
-
2
-
-
1
-
-
1
-
-
3
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
3
-
-
-
-
2
-
2
-
1
1
3
-
-
-
1
-
1
-
-
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
286395
Yaniv
Aromatic biosynthesis. XIV. 5- ...
Escherichia coli
J. Biol. Chem.
213
787-795
1955
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-