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show all sequences of 2.7.1.71

Shikimate kinase (EC 2.7.1.71) from Mycobacterium tuberculosis: kinetics and structural dynamics of a potential molecular target for drug development

Saidemberg, D.M.; Passarelli, A.W.; Rodrigues, A.V.; Basso, L.A.; Santos, D.S.; Palma, M.S.; Curr. Med. Chem. 18, 1299-1310 (2011)

Data extracted from this reference:

Application
Application
Commentary
Organism
drug development
the enzyme is a target for antimicrobial and anti-paarasite drugs
Mycobacterium tuberculosis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis and conformational dynamics, overview
Mycobacterium tuberculosis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + shikimate
Mycobacterium tuberculosis
-
ADP + 3-phosphoshikimate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + shikimate
-
722086
Mycobacterium tuberculosis
ADP + 3-phosphoshikimate
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Mycobacterium tuberculosis
Application (protein specific)
Application
Commentary
Organism
drug development
the enzyme is a target for antimicrobial and anti-paarasite drugs
Mycobacterium tuberculosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Mycobacterium tuberculosis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis and conformational dynamics, overview
Mycobacterium tuberculosis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + shikimate
Mycobacterium tuberculosis
-
ADP + 3-phosphoshikimate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + shikimate
-
722086
Mycobacterium tuberculosis
ADP + 3-phosphoshikimate
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
the enzyme catalyzes the fifth step in the shikimate pathway
Mycobacterium tuberculosis
physiological function
he phosphate binding domain in the apo-enzyme is fairly rigid and largely protected from solvent access, even at relatively high temperatures. The shikimate binding domain is highly flexible, the apo-enzyme tends to exhibit large conformational changes to permit LID closure after the shikimate binding. The nucleotide binding domain is initially conformationally rigid, which seems to favour the initial orientation of ADP/ATP, but becomes highly flexible at temperatures above 30°C, which may permit domain rotation. Part of the LID domain, including the phosphate binding site, is partially rigid, while another part is highly flexible and accessible to the solvent, mide H/D exchange and mass spectrometry
Mycobacterium tuberculosis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme catalyzes the fifth step in the shikimate pathway
Mycobacterium tuberculosis
physiological function
he phosphate binding domain in the apo-enzyme is fairly rigid and largely protected from solvent access, even at relatively high temperatures. The shikimate binding domain is highly flexible, the apo-enzyme tends to exhibit large conformational changes to permit LID closure after the shikimate binding. The nucleotide binding domain is initially conformationally rigid, which seems to favour the initial orientation of ADP/ATP, but becomes highly flexible at temperatures above 30°C, which may permit domain rotation. Part of the LID domain, including the phosphate binding site, is partially rigid, while another part is highly flexible and accessible to the solvent, mide H/D exchange and mass spectrometry
Mycobacterium tuberculosis
Other publictions for EC 2.7.1.71
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)
737517
Rajput
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1
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5
2
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2
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162
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2
2
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738850
Prado
Targeting the motion of shikim ...
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J. Med. Chem.
59
5471-5487
2016
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28
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3
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11
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26
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3
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3
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737351
Sutton
Structure of shikimate kinase, ...
Acinetobacter baumannii, Acinetobacter baumannii 307-0294
Acta Crystallogr. Sect. D
71
1736-1744
2015
-
-
1
1
-
-
1
1
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1
1
2
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5
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1
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1
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1
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737396
Liu
-
Isolation and in silico charac ...
Senna obtusifolia
Acta Physiol. Plant.
37
85
2015
-
-
-
-
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-
-
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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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737442
Simithy
Development of an ESI-LC-MS-ba ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Anal. Chem.
87
2129-2136
2015
-
-
-
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2
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161
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739757
Liu
Metabolic engineering of Esche ...
Escherichia coli, Escherichia coli JW0379-1
World J. Microbiol. Biotechnol.
30
2543-2550
2014
-
-
1
-
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738446
Blanco
Mycobacterium tuberculosis shi ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Am. Chem. Soc.
135
12366-12376
2013
-
-
-
1
-
-
5
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2
-
11
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2
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739394
Hsu
Pathway-based screening strate ...
Helicobacter pylori
PLoS Comput. Biol.
9
e1003127
2013
-
-
-
-
-
-
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1
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2
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739462
Rosado
The mode of action of recombin ...
Mycobacterium tuberculosis
PLoS ONE
8
e61918
2013
-
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1
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2
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1
2
1
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3
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1
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1
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1
1
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2
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2
2
721852
Chen
Deletion of the aroK gene is e ...
Escherichia coli, Escherichia coli DHPYA-T7
Biores. Technol.
119
141-147
2012
-
1
1
-
1
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1
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2
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3
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2
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1
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1
1
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721930
Kenyon
The role of the C8 proton of A ...
Mycobacterium tuberculosis
BMC Biochem.
13
15
2012
-
-
1
-
6
-
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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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6
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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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2
2
-
-
-
723010
Vianna
Identification of new potentia ...
Mycobacterium tuberculosis
J. Mol. Model.
18
755-764
2012
-
1
-
-
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-
11
-
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1
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1
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4
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2
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11
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1
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1
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2
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-
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4
4
-
-
-
723553
Cheng
Structures of Helicobacter pyl ...
Helicobacter pylori
PLoS ONE
7
e33481
2012
-
-
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1
12
1
1
7
-
1
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1
-
5
-
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1
1
1
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1
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1
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1
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1
1
12
1
1
1
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7
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1
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1
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1
1
1
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1
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2
2
-
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722086
Saidemberg
Shikimate kinase (EC 2.7.1.71) ...
Mycobacterium tuberculosis
Curr. Med. Chem.
18
1299-1310
2011
-
1
-
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1
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1
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1
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2
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2
2
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723722
Fucile
Structural and biochemical inv ...
Arabidopsis thaliana
Protein Sci.
20
1125-1136
2011
-
-
1
1
8
-
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1
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1
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4
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2
1
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1
8
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2
1
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1
3
3
1
-
-
722010
Kumar
Structure-based in silico desi ...
Mycobacterium tuberculosis
Chem. Biol. Drug Des.
76
277-284
2010
-
1
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2
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1
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1
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4
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1
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-
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2
2
-
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-
722422
Arora
In silico characterization of ...
Shigella flexneri, Shigella flexneri 8401
Interdiscip. Sci.
2
280-290
2010
-
1
-
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1
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1
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2
2
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1
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1
1
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691236
Pauli
Molecular modeling and dynamic ...
Bacillus anthracis
Bioorg. Med. Chem.
16
8098-8108
2008
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1
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4
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691278
Segura-Cabrera
Structure-based prediction of ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Bioorg. Med. Chem. Lett.
18
3152-3157
2008
-
-
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10
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9
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10
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706409
Fucile
Evolutionary diversification o ...
Arabidopsis thaliana
PLoS Genet.
4
e1000292
2008
-
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-
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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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1
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-
671157
Dias
Effects of the magnesium and c ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
F63
1-6
2007
-
-
1
1
-
-
-
-
-
2
-
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11
-
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1
-
-
-
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1
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1
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1
1
1
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2
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1
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1
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672569
Han
Discovery of Helicobacter pylo ...
Helicobacter pylori, Helicobacter pylori SS1
Bioorg. Med. Chem.
15
656-662
2007
-
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1
1
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2
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1
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4
-
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1
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2
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1
2
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2
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1
1
1
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2
2
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673192
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Shikimate kinase: a potential ...
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Crystal structure of Mycobacte ...
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Structural basis for shikimate ...
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663189
Kasai
Identification of three shikim ...
Oryza sativa
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2005
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660595
Pereira
Structure of shikimate kinase ...
Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
60
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2004
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2004
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661744
Dhaliwal
Crystallographic studies of sh ...
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FEBS Lett.
574
49-54
2004
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641900
Cerasoli
Effects of salts on the functi ...
Dickeya chrysanthemi
Biochim. Biophys. Acta
1648
43-54
2003
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1
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641908
Romanowski
Crystal structure of the Esche ...
Escherichia coli
Proteins Struct. Funct. Genet.
47
558-562
2002
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Gu
Crystal structure of shikimate ...
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2002
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641913
Cerasoli
The refolding of type II shiki ...
Dickeya chrysanthemi
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269
2124-2132
2002
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638205
Oliveira
Cloning and Overexpression in ...
Mycobacterium tuberculosis
Protein Expr. Purif.
22
430-435
2001
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641912
Daugherty
Archaeal shikimate kinase, a n ...
Methanocaldococcus jannaschii
J. Bacteriol.
183
292-300
2001
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641915
Krell
Biochemical and X-ray crystall ...
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1137-1149
2001
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The three-dimensional structur ...
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1998
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641910
Krell
Crystallization and preliminar ...
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Acta Crystallogr. Sect. D
53
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1997
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Idziak
The interaction of shikimate k ...
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Biochem. Soc. Trans.
25
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1997
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A reassessment of the relation ...
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Identification of the gene (ar ...
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Shikimate kinase from spinach ...
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Shikimate kinases from Escheri ...
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Duncan
The pentafunctional arom enzym ...
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DeFeyter
Purification and properties of ...
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641899
Bode
Purification and isolation of ...
Schizosaccharomyces pombe
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289-296
1983
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641901
Kempner
The functional unit of the aro ...
Neurospora crassa
J. Biol. Chem.
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1982
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5468
Bode
Aggregation und Trennbarkeit d ...
Cyberlindnera fabianii, Cyberlindnera jadinii, Hansenula henricii, Lodderomyces elongisporus, Meyerozyma guilliermondii, Neurospora crassa, Rhodotorula mucilaginosa, Rhodotorula sphaerocarpa, Rhodotorula toruloides, Saccharomyces cerevisiae, Saccharomycopsis lipolytica, Wickerhamomyces anomalus
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Koshiba
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Alicyclic acid metabolism in p ...
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Bowen
In vivo activity, purification ...
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Morell
Shikimate kinase isoenzymes in ...
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1968
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