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show all sequences of 1.1.1.25

A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass

Singh, S.; Stavrinides, J.; Christendat, D.; Guttman, D.S.; Mol. Biol. Evol. 25, 2221-2232 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
five putative SDH-encoding genes amplified and cloned into either a modified pET28a vector or the p15TVLIC vector, a ligation-independent vector due to incompatible cloning sites between the insert and pET28.3. Expressed in either the Escherichia coli strain BL21 gold (p15TV-LIC constructs) or the Escherichia coli BL21CodonPlus (pET28.3constructs); five putative SDH-encoding genes amplified and cloned into either a modified pET28a vector or the p15TVLIC vector, a ligation-independent vector due to incompatible cloning sites between the insert and pET28.3. Expressed in either the Escherichia coli strain BL21 gold (p15TV-LIC constructs) or the Escherichia coli BL21CodonPlus (pET28.3constructs)
Pseudomonas putida KT2440
SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into a vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.; SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into a vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.; SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.; SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.; SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0046
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
0.0073
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
0.0786
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
0.0786
-
shikimate
in the presence of 2 mM NAD+
Pseudomonas putida KT2440
0.105
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
0.105
-
shikimate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
0.112
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
0.112
-
NADP+
in the presence of shikimate
Pseudomonas putida KT2440
0.351
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
0.572
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
0.783
-
quinate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
1.083
-
NAD+
pH 8.8, presence of 2 mM quinate
Pseudomonas putida
4.2
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
5.4
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
5.43
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
5.43
-
NAD+
in the presence of shikimate
Pseudomonas putida KT2440
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
quinate + NAD+
Pseudomonas putida
the fourth enzyme in the shikimate pathway
3-dehydroquinate + NADH + H+
-
-
r
shikimate + NAD+
Pseudomonas putida
-
3-dehydroshikimate + NADH + H+
-
-
r
shikimate + NAD+
Pseudomonas putida KT2240
-
3-dehydroshikimate + NADH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida
the fourth enzyme in the shikimate pathway
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida KT2240
the fourth enzyme in the shikimate pathway
3-dehydroshikimate + NADPH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
Q88GF6
homolog sdhL; strain KT2440
-
Pseudomonas putida
Q88IJ7
homolog ael1; strain KT2240
-
Pseudomonas putida
Q88JP1
homolog rifl; strain KT2440
-
Pseudomonas putida
Q88K85
homolog ydiB; strain KT2440
-
Pseudomonas putida
Q88RQ5
homolog aroE; strain KT2440
-
Pseudomonas putida KT2240
Q88IJ7
homolog ael1; strain KT2240
-
Pseudomonas putida KT2440
Q88IJ7
-
-
Pseudomonas putida KT2440
Q88RQ5
-
-
Purification (Commentary)
Commentary
Organism
by nickel-nitrilotriacetic acid affinity chromatography; by nickel-nitrilotriacetic acid affinity chromatography
Pseudomonas putida KT2440
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4 °C in 10 mM Tris–HCl, 500 mM NaCl, and 5% glycerol.; Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4 °C in 10 mM Tris–HCl, 500 mM NaCl, and 5% glycerol.; Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM Tris-HCl, 500 mM NaCl, and 5% glycerol.; Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM Tris–HCl, 500 mM NaCl, and 5% glycerol.; Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM Tris–HCl, 500 mM NaCl, and 5% glycerol.
Pseudomonas putida
Storage Stability
Storage Stability
Organism
4°C, 10 mM Tris-HCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
Pseudomonas putida KT2440
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
694093
Pseudomonas putida KT2440
?
-
-
-
-
quinate + NAD(P)+
-
694093
Pseudomonas putida KT2440
3-dehydroquinate + NAD(P)H + H+
-
-
-
?
quinate + NAD+
the fourth enzyme in the shikimate pathway
694093
Pseudomonas putida
3-dehydroquinate + NADH + H+
-
-
-
r
shikimate + NAD(P)+
-
694093
Pseudomonas putida KT2440
3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD+
-
694093
Pseudomonas putida
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
-
694093
Pseudomonas putida KT2240
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
the fourth enzyme in the shikimate pathway
694093
Pseudomonas putida
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
the fourth enzyme in the shikimate pathway
694093
Pseudomonas putida KT2240
3-dehydroshikimate + NADPH + H+
-
-
-
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at; assay at; assay at; assay at
Pseudomonas putida
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.077
-
NADP+
in the presence of quinate
Pseudomonas putida KT2440
0.16
-
quinate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
1.99
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
1.99
-
shikimate
in the presence of 2 mM NAD+
Pseudomonas putida KT2440
5.3
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
5.3
-
NADP+
in the presence of shikimate
Pseudomonas putida KT2440
5.8
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
5.8
-
shikimate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
6.72
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
6.72
-
NAD+
in the presence of shikimate
Pseudomonas putida KT2440
31.2
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
31.2
-
shikimate
in the presence of 2 mM NAD+
Pseudomonas putida KT2440
37.7
-
quinate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
40.7
-
NAD+
pH 8.8, presence of 2 mM quinate
Pseudomonas putida
55.7
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
61.1
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
97.1
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
97.1
-
NAD+
in the presence of shikimate
Pseudomonas putida KT2440
261.5
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
261.5
-
NADP+
in the presence of shikimate
Pseudomonas putida KT2440
266.2
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
266.2
-
shikimate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
assay at; assay at; assay at; assay at
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
NAD(P)+
;
Pseudomonas putida KT2440
NAD+
-
Pseudomonas putida
NADP+
;
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
five putative SDH-encoding genes amplified and cloned into either a modified pET28a vector or the p15TVLIC vector, a ligation-independent vector due to incompatible cloning sites between the insert and pET28.3. Expressed in either the Escherichia coli strain BL21 gold (p15TV-LIC constructs) or the Escherichia coli BL21CodonPlus (pET28.3constructs)
Pseudomonas putida KT2440
SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into a vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.
Pseudomonas putida
SDH-encoding gene is amplified by polymerase chain reaction from Pseudomonas putida KT2440 genomic DNA using primers with incorporated restriction sites. Resulting product is cloned into vector and expressed in the Escherichia coli strain BL21 with appropriate antibiotics.
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD(P)+
-
Pseudomonas putida KT2440
NAD+
-
Pseudomonas putida
NADP+
-
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0046
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
0.0073
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
0.0786
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
0.0786
-
shikimate
in the presence of 2 mM NAD+
Pseudomonas putida KT2440
0.105
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
0.105
-
shikimate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
0.112
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
0.112
-
NADP+
in the presence of shikimate
Pseudomonas putida KT2440
0.351
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
0.572
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
0.783
-
quinate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
1.083
-
NAD+
pH 8.8, presence of 2 mM quinate
Pseudomonas putida
4.2
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
5.4
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
5.43
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
5.43
-
NAD+
in the presence of shikimate
Pseudomonas putida KT2440
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
quinate + NAD+
Pseudomonas putida
the fourth enzyme in the shikimate pathway
3-dehydroquinate + NADH + H+
-
-
r
shikimate + NAD+
Pseudomonas putida
-
3-dehydroshikimate + NADH + H+
-
-
r
shikimate + NAD+
Pseudomonas putida KT2240
-
3-dehydroshikimate + NADH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida
the fourth enzyme in the shikimate pathway
3-dehydroshikimate + NADPH + H+
-
-
r
shikimate + NADP+
Pseudomonas putida KT2240
the fourth enzyme in the shikimate pathway
3-dehydroshikimate + NADPH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
by nickel-nitrilotriacetic acid affinity chromatography
Pseudomonas putida KT2440
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4 °C in 10 mM Tris–HCl, 500 mM NaCl, and 5% glycerol.
Pseudomonas putida
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM Tris-HCl, 500 mM NaCl, and 5% glycerol.
Pseudomonas putida
Cultures with expressed SDH enzymes are incubated and then induced with 0.4 mM isopropyl-beta-D-thiogalactopyranoside. Harvested cells are disrupted and the insoluble cellular material is removed by centrifugation. The recombinants are purified from other contaminating proteins using nickel-nitrilotriacetic acid affinity chromatography. Protein samples for kinetic studies are dialyzed and stored at 4°C in 10 mM Tris–HCl, 500 mM NaCl, and 5% glycerol.
Pseudomonas putida
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 10 mM Tris-HCl buffer, pH 7.5, 500 mM NaCl, 5% glycerol
Pseudomonas putida KT2440
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
694093
Pseudomonas putida KT2440
?
-
-
-
-
quinate + NAD(P)+
-
694093
Pseudomonas putida KT2440
3-dehydroquinate + NAD(P)H + H+
-
-
-
?
quinate + NAD+
the fourth enzyme in the shikimate pathway
694093
Pseudomonas putida
3-dehydroquinate + NADH + H+
-
-
-
r
shikimate + NAD(P)+
-
694093
Pseudomonas putida KT2440
3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD+
-
694093
Pseudomonas putida
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
-
694093
Pseudomonas putida KT2240
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+
the fourth enzyme in the shikimate pathway
694093
Pseudomonas putida
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
the fourth enzyme in the shikimate pathway
694093
Pseudomonas putida KT2240
3-dehydroshikimate + NADPH + H+
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Pseudomonas putida
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.077
-
NADP+
in the presence of quinate
Pseudomonas putida KT2440
0.16
-
quinate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
1.99
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
1.99
-
shikimate
in the presence of 2 mM NAD+
Pseudomonas putida KT2440
5.3
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
5.3
-
NADP+
in the presence of shikimate
Pseudomonas putida KT2440
5.8
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
5.8
-
shikimate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
6.72
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
6.72
-
NAD+
in the presence of shikimate
Pseudomonas putida KT2440
31.2
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
31.2
-
shikimate
in the presence of 2 mM NAD+
Pseudomonas putida KT2440
37.7
-
quinate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
40.7
-
NAD+
pH 8.8, presence of 2 mM quinate
Pseudomonas putida
55.7
-
shikimate
pH 8.8, presence of 2 mM NAD+
Pseudomonas putida
61.1
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
97.1
-
NAD+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
97.1
-
NAD+
in the presence of shikimate
Pseudomonas putida KT2440
261.5
-
NADP+
pH 8.8, presence of 2 mM shikimate
Pseudomonas putida
261.5
-
NADP+
in the presence of shikimate
Pseudomonas putida KT2440
266.2
-
shikimate
pH 8.8, presence of 2 mM NADP+
Pseudomonas putida
266.2
-
shikimate
in the presence of 2 mM NADP+
Pseudomonas putida KT2440
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
assay at
Pseudomonas putida
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
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1
-
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6
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1
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5
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-
-
-
-
12
1
-
-
-
6
4
-
-
5
-
-
-
-
-
2
6
-
-
-
-
4
-
6
-
-
2
-
-
-
-
-
-
-
-
-
12
2
-
-
-
6
4
-
-
-
1
1
1
1
6
6
725977
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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
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-
1
1
1
-
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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Rodrigues
The conserved Lysine69 residue ...
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Schoepe
1.6 A structure of an NAD(+)-d ...
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Structural studies of shikimat ...
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A phylogenomic analysis of the ...
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Functional analysis of the ess ...
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Fonseca
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Mycobacterium tuberculosis
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Gan
Structural and biochemical ana ...
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Singh
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The DHQ-dehydroshikimate-SDH-s ...
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16
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Schoepe
Cloning, expression, purificat ...
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Singh
Structure of Arabidopsis dehyd ...
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1
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1
2
1
10
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18
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2
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1
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3
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1
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18
1
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Adachi
Purification and properties of ...
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2
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2
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Biochemical characterization a ...
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2
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1
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657359
Padyana
Crystal structure of shikimate ...
Methanocaldococcus jannaschii
Structure
11
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2003
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670901
Vogan
Shikimate dehydrogenase struct ...
Methanocaldococcus jannaschii
Structure
11
902-903
2003
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Magalhaes
Cloning and expression of func ...
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Protein Expr. Purif.
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Maclean
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Diaz
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Shikimate dehydrogenase from p ...
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Inhibition of shikimate dehydr ...
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286387
Lourenco
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Partial purification and some ...
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Phytochemistry
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1984
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Polley
Purification and characterizat ...
Physcomitrella patens
Biochim. Biophys. Acta
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1978
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286388
Koshiba
Purification of two forms of t ...
Vigna mungo
Biochim. Biophys. Acta
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1978
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Jacobson
Purification and stability of ...
Neurospora crassa
Biochim. Biophys. Acta
289
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1972
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286390
Higuchi
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Changes in activity of shikima ...
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1967
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286389
Sanderson
5-Dehydroshikimate reductase i ...
Camellia sinensis
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1966
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Balinsky
Aromatic biosynthesis in highe ...
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Yaniv
Aromatic biosynthesis. XIV. 5- ...
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1955
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