BRENDA - Enzyme Database
show all sequences of 1.1.1.169

Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP(.)

Aikawa, Y.; Nishitani, Y.; Tomita, H.; Atomi, H.; Miki, K.; Acta crystallogr. Sect. F 72, 369-375 (2016)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene TK1968, recombinant coexpression of wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer in Escherichia coli
Thermococcus kodakarensis
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant tagged enzyme mutant C84A, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg /ml protein in 10 mM Tris-HCl, pH 8.0, 1 mM dithiothreitol, mM NADH, and 1 mM 2-oxopantoate, with 0.001 ml of reservoir solution containing 100 mM sodium acetate, pH 5.5, 10% w/v PEG 3350, 20% v/v 2-propanol, and equilibration against 0.5 ml reservoir solution, at 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method for modeling
Thermococcus kodakarensis
Engineering
Protein Variants
Commentary
Organism
C84A
site-directed mutagenesis
Thermococcus kodakarensis
W129A
site-directed mutagenesis
Thermococcus kodakarensis
Y60A
site-directed mutagenesis
Thermococcus kodakarensis
Inhibitors
Inhibitors
Commentary
Organism
Structure
CoA
feedback inhibition
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(R)-pantoate + NADP+
Thermococcus kodakarensis
-
2-dehydropantoate + NADPH + H+
-
-
r
(R)-pantoate + NADP+
Thermococcus kodakarensis ATCC BAA-918
-
2-dehydropantoate + NADPH + H+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Thermococcus kodakarensis
Q5JGC2
-
-
Thermococcus kodakarensis ATCC BAA-918
Q5JGC2
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer from Escherichia coli by affinity chromatography
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(R)-pantoate + NADP+
-
739822
Thermococcus kodakarensis
2-dehydropantoate + NADPH + H+
-
-
-
r
(R)-pantoate + NADP+
-
739822
Thermococcus kodakarensis ATCC BAA-918
2-dehydropantoate + NADPH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
crystal structure analysis
Thermococcus kodakarensis
Synonyms
Synonyms
Commentary
Organism
ketopantoate reductase
-
Thermococcus kodakarensis
KPR
-
Thermococcus kodakarensis
Tk-KPR
-
Thermococcus kodakarensis
TK1968
-
Thermococcus kodakarensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Thermococcus kodakarensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.4
-
assay at
Thermococcus kodakarensis
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene TK1968, recombinant coexpression of wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer in Escherichia coli
Thermococcus kodakarensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Thermococcus kodakarensis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant tagged enzyme mutant C84A, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg /ml protein in 10 mM Tris-HCl, pH 8.0, 1 mM dithiothreitol, mM NADH, and 1 mM 2-oxopantoate, with 0.001 ml of reservoir solution containing 100 mM sodium acetate, pH 5.5, 10% w/v PEG 3350, 20% v/v 2-propanol, and equilibration against 0.5 ml reservoir solution, at 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method for modeling
Thermococcus kodakarensis
Engineering (protein specific)
Protein Variants
Commentary
Organism
C84A
site-directed mutagenesis
Thermococcus kodakarensis
W129A
site-directed mutagenesis
Thermococcus kodakarensis
Y60A
site-directed mutagenesis
Thermococcus kodakarensis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CoA
feedback inhibition
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(R)-pantoate + NADP+
Thermococcus kodakarensis
-
2-dehydropantoate + NADPH + H+
-
-
r
(R)-pantoate + NADP+
Thermococcus kodakarensis ATCC BAA-918
-
2-dehydropantoate + NADPH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer from Escherichia coli by affinity chromatography
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(R)-pantoate + NADP+
-
739822
Thermococcus kodakarensis
2-dehydropantoate + NADPH + H+
-
-
-
r
(R)-pantoate + NADP+
-
739822
Thermococcus kodakarensis ATCC BAA-918
2-dehydropantoate + NADPH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
crystal structure analysis
Thermococcus kodakarensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Thermococcus kodakarensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.4
-
assay at
Thermococcus kodakarensis
General Information
General Information
Commentary
Organism
physiological function
ketopantoate reductase catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate which is a step in the biosynthesis of coenzyme A
Thermococcus kodakarensis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
ketopantoate reductase catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate which is a step in the biosynthesis of coenzyme A
Thermococcus kodakarensis
Other publictions for EC 1.1.1.169
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)
739822
Aikawa
Crystal structure of ketopanto ...
Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918
Acta crystallogr. Sect. F
72
369-375
2016
-
-
1
1
3
-
1
-
-
-
-
2
-
9
-
-
1
-
-
-
-
-
2
1
4
1
-
-
-
1
-
-
1
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-
1
1
1
3
-
-
1
-
-
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2
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1
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-
2
1
1
-
-
-
1
-
-
-
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1
1
-
-
-
741385
Aikawa
Crystal structure of archaeal ...
Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918
Proteins
84
374-382
2016
-
-
1
1
1
-
1
-
-
-
-
2
-
13
-
-
1
-
-
-
-
-
4
1
4
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
1
-
-
1
-
-
-
-
-
2
-
-
-
1
-
-
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-
4
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
740065
Sanchez
Evidence of kinetic cooperativ ...
Staphylococcus aureus
Biochemistry
54
3360-3369
2015
-
-
2
2
2
-
1
5
-
-
-
2
-
6
-
-
2
1
-
-
-
-
2
3
2
1
-
-
4
1
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-
1
1
-
-
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-
2
1
2
2
-
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1
1
5
-
-
-
2
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-
-
2
-
-
-
-
2
3
1
-
-
4
1
-
-
-
-
4
4
-
-
-
725293
Miller
PanG, a new ketopantoate reduc ...
Francisella tularensis subsp. novicida
J. Bacteriol.
195
965-976
2013
-
-
-
-
-
-
-
-
-
-
-
-
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25
-
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-
-
-
-
-
-
-
-
3
-
-
-
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-
-
-
-
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-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
729136
Miyanaga
The crystal structure of D-man ...
Enterococcus faecalis, Enterococcus faecalis IAM10071
Biochem. Biophys. Res. Commun.
439
109-114
2013
-
-
-
-
-
-
-
-
-
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-
2
-
4
-
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2
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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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-
-
-
-
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-
-
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-
-
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-
736827
Tomita
Identification and characteriz ...
Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918
Mol. Microbiol.
90
307-321
2013
-
-
1
-
1
-
1
7
-
-
2
4
-
19
-
-
1
-
-
-
-
-
13
1
5
1
1
1
6
1
-
-
4
1
-
-
-
-
1
4
-
1
-
-
1
1
7
-
-
2
4
-
-
-
1
-
-
-
-
13
1
1
1
1
6
1
-
-
-
-
2
2
-
6
6
696603
Headey
Backbone assignments of the 34 ...
Escherichia coli
Biomol. NMR Assign.
2
93-96
2008
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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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1
-
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-
-
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-
-
-
-
-
-
-
-
-
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684140
Ciulli
pH-tuneable binding of 2-phosp ...
Escherichia coli
Acta Crystallogr. Sect. D
63
171-178
2007
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1
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1
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4
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3
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3
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1
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1
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1
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3
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687675
Ciulli
Crystal structure of Escherich ...
Escherichia coli
J. Biol. Chem.
282
8487-8497
2007
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1
1
6
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3
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1
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4
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2
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2
1
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2
1
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2
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1
2
1
6
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3
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1
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2
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1
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2
1
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669806
Ciulli
Probing hot spots at protein-l ...
Escherichia coli
J. Med. Chem.
49
4992-5000
2006
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7
1
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1
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4
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1
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2
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2
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1
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3
6
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3
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7
6
1
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1
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2
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1
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667561
Ciulli
Biophysical tools to monitor e ...
Escherichia coli
Biochem. Soc. Trans.
33
767-771
2005
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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
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667687
Lobley
The crystal structure of Esche ...
Escherichia coli
Biochemistry
44
8930-8939
2005
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1
1
7
-
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1
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1
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4
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1
1
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2
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2
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2
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1
2
1
7
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1
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1
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1
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2
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654677
Zheng
Substrate specificity and kine ...
Escherichia coli
Biochemistry
42
11289-11296
2003
-
-
1
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-
-
8
-
-
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1
-
4
-
-
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7
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1
1
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1
1
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4
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1
4
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8
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1
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7
-
1
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-
-
1
1
-
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-
-
-
-
-
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656330
Merkamm
Ketopantoate reductase activit ...
Corynebacterium glutamicum
J. Biotechnol.
104
253-260
2003
-
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1
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1
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1
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9
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2
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2
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4
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1
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1
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2
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2
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286110
Matak-Vinkovic
Crystal structure of Escherich ...
Stenotrophomonas maltophilia, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli, Stenotrophomonas maltophilia 845
Biochemistry
40
14493-14500
2001
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1
1
1
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4
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2
4
2
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9
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1
1
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2
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4
4
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2
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3
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1
3
1
1
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4
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2
4
2
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1
1
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2
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4
4
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-
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2
-
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-
-
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286108
Zheng
Kinetic and mechanistic analys ...
Escherichia coli
Biochemistry
39
3708-3717
2000
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1
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-
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2
4
-
1
4
1
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4
-
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1
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1
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2
1
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2
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1
2
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2
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4
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1
4
1
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1
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1
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2
1
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-
-
-
-
-
-
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-
-
-
-
286109
Zheng
Identification of active site ...
Escherichia coli
Biochemistry
39
16244-16251
2000
5
-
1
-
10
-
-
12
-
1
1
-
-
6
-
-
1
-
-
-
1
-
2
1
-
-
-
-
-
1
-
-
2
-
-
-
5
-
1
2
-
10
-
-
-
-
12
-
1
1
-
-
-
-
1
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
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286106
Elischewski
Pantothenate production in Esc ...
Escherichia coli
J. Biotechnol.
75
135-146
1999
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1
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-
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1
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10
-
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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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286107
Frodyma
ApbA, the ketopantoate reducta ...
Saccharomyces cerevisiae, Escherichia coli, Stenotrophomonas maltophilia, Salmonella enterica subsp. enterica serovar Typhimurium, Stenotrophomonas maltophilia 845, Escherichia coli BL21/lambdaDE3
J. Biol. Chem.
273
5572-5576
1998
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1
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-
-
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2
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1
3
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15
-
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1
-
-
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6
-
12
2
-
1
-
-
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1
-
-
8
-
-
-
-
-
1
8
-
-
-
-
-
-
2
-
-
1
3
-
-
-
1
-
-
6
-
12
2
1
-
-
-
1
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-
-
-
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-
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-
286102
Kataoka
-
Novel enzymic production of D- ...
Agrobacterium tumefaciens, Agrobacterium sp., Pseudomonas putida, Stenotrophomonas maltophilia
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54
177-182
1990
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4
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4
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2
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-
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3
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3
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-
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-
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4
-
2
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286103
Shimizu
Ketopantoic acid reductase of ...
Saccharomyces cerevisiae, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia 845
J. Biol. Chem.
263
12077-12084
1988
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-
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1
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10
4
-
1
4
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-
10
-
-
1
-
-
-
2
1
6
1
-
1
1
3
-
2
-
2
4
-
-
-
-
-
-
4
1
-
-
-
10
-
4
-
1
4
-
-
-
-
1
-
-
2
1
6
1
1
1
3
-
2
-
2
-
-
-
-
-
-
-
286105
Wilken
Ketopantoic acid and ketopanto ...
Saccharomyces cerevisiae, Escherichia coli
J. Biol. Chem.
250
2311-2314
1975
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-
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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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-
-
2
-
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-
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286104
King
-
Separation and preliminary stu ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae NRRL Y-2034
J. Biol. Chem.
247
4096-4098
1972
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2
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1
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2
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4
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2
1
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2
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2
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1
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2
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4
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2
1
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