BRENDA - Enzyme Database show
show all sequences of 1.1.1.169

Identification and characterization of an archaeal ketopantoate reductase and its involvement in regulation of coenzyme A biosynthesis

Tomita, H.; Imanaka, T.; Atomi, H.; Mol. Microbiol. 90, 307-321 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene TK1968, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli
Thermococcus kodakarensis
Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of a gene TK1968 disruption mutant
Thermococcus kodakarensis
Inhibitors
Inhibitors
Commentary
Organism
Structure
CoA
strong inhibition, competitive versus NADH, effect on enzyme kinetics, overview
Thermococcus kodakarensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics in both reaction directions
Thermococcus kodakarensis
0.00135
-
NADPH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.003
-
NADH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.006
-
2-dehydropantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.041
-
NAD+
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.13
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
2.04
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34048
-
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
Thermococcus kodakarensis
60000
-
recombinant enzyme, gel filtration
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-pantoate + NAD+
Thermococcus kodakarensis
-
2-dehydropantoate + NADH + H+
-
-
r
(R)-pantoate + NAD+
Thermococcus kodakarensis KUW1
-
2-dehydropantoate + NADH + H+
-
-
r
2-dehydropantoate + NADH + H+
Thermococcus kodakarensis
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
(R)-pantoate + NAD+
-
-
r
2-dehydropantoate + NADH + H+
Thermococcus kodakarensis KUW1
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
(R)-pantoate + NAD+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermococcus kodakarensis
Q5JGC2
gene TK1968
-
Thermococcus kodakarensis KUW1
Q5JGC2
gene TK1968
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli by heat treatment, anion-exchange chromatography, and gel filtration
Thermococcus kodakarensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantoate + NAD+
-
736827
Thermococcus kodakarensis
2-dehydropantoate + NADH + H+
-
-
-
r
(R)-pantoate + NAD+
-
736827
Thermococcus kodakarensis KUW1
2-dehydropantoate + NADH + H+
-
-
-
r
(R)-pantoate + NADP+
-
736827
Thermococcus kodakarensis
2-dehydropantoate + NADPH + H+
-
-
-
r
(R)-pantoate + NADP+
-
736827
Thermococcus kodakarensis KUW1
2-dehydropantoate + NADPH + H+
-
-
-
r
(S)-pantoate + NAD+
low activity
736827
Thermococcus kodakarensis
2-dehydropantoate + NADH + H+
-
-
-
r
(S)-pantoate + NADP+
low activity
736827
Thermococcus kodakarensis
2-dehydropantoate + NADPH + H+
-
-
-
r
2-dehydropantoate + NADH + H+
-
736827
Thermococcus kodakarensis
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADH + H+
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
736827
Thermococcus kodakarensis
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADH + H+
-
736827
Thermococcus kodakarensis KUW1
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADH + H+
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
736827
Thermococcus kodakarensis KUW1
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADPH + H+
-
736827
Thermococcus kodakarensis
(R)-pantoate + NADP+
-
-
-
r
additional information
D-pantoate is much more preferred over L-pantoate in the reduction reaction, suggesting that the enzyme generates D-pantoate from 2-oxopantoate in the oxidation reaction
736827
Thermococcus kodakarensis
?
-
-
-
-
additional information
D-pantoate is much more preferred over L-pantoate in the reduction reaction, suggesting that the enzyme generates D-pantoate from 2-oxopantoate in the oxidation reaction
736827
Thermococcus kodakarensis KUW1
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
homodimer
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
Thermococcus kodakarensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
recombinant enzyme
Thermococcus kodakarensis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
50
110
and above, activity range, profile overview
Thermococcus kodakarensis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
90
purified recombinant enzyme, pH 6.4, completely stable at for at least 24 h
Thermococcus kodakarensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.22
-
NADPH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
2.41
-
NAD+
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
3.17
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
3.8
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
19.7
-
NADH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
23.1
-
2-dehydropantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.4
-
recombinant enzyme
Thermococcus kodakarensis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Thermococcus kodakarensis
NADH
preferred cofactor compared to NADPH
Thermococcus kodakarensis
NADP+
-
Thermococcus kodakarensis
NADPH
-
Thermococcus kodakarensis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000042
-
CoA
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene TK1968, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli
Thermococcus kodakarensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Thermococcus kodakarensis
NADH
preferred cofactor compared to NADPH
Thermococcus kodakarensis
NADP+
-
Thermococcus kodakarensis
NADPH
-
Thermococcus kodakarensis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of a gene TK1968 disruption mutant
Thermococcus kodakarensis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CoA
strong inhibition, competitive versus NADH, effect on enzyme kinetics, overview
Thermococcus kodakarensis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000042
-
CoA
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics in both reaction directions
Thermococcus kodakarensis
0.00135
-
NADPH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.003
-
NADH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.006
-
2-dehydropantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.041
-
NAD+
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
0.13
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
2.04
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34048
-
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
Thermococcus kodakarensis
60000
-
recombinant enzyme, gel filtration
Thermococcus kodakarensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-pantoate + NAD+
Thermococcus kodakarensis
-
2-dehydropantoate + NADH + H+
-
-
r
(R)-pantoate + NAD+
Thermococcus kodakarensis KUW1
-
2-dehydropantoate + NADH + H+
-
-
r
2-dehydropantoate + NADH + H+
Thermococcus kodakarensis
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
(R)-pantoate + NAD+
-
-
r
2-dehydropantoate + NADH + H+
Thermococcus kodakarensis KUW1
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
(R)-pantoate + NAD+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli by heat treatment, anion-exchange chromatography, and gel filtration
Thermococcus kodakarensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-pantoate + NAD+
-
736827
Thermococcus kodakarensis
2-dehydropantoate + NADH + H+
-
-
-
r
(R)-pantoate + NAD+
-
736827
Thermococcus kodakarensis KUW1
2-dehydropantoate + NADH + H+
-
-
-
r
(R)-pantoate + NADP+
-
736827
Thermococcus kodakarensis
2-dehydropantoate + NADPH + H+
-
-
-
r
(R)-pantoate + NADP+
-
736827
Thermococcus kodakarensis KUW1
2-dehydropantoate + NADPH + H+
-
-
-
r
(S)-pantoate + NAD+
low activity
736827
Thermococcus kodakarensis
2-dehydropantoate + NADH + H+
-
-
-
r
(S)-pantoate + NADP+
low activity
736827
Thermococcus kodakarensis
2-dehydropantoate + NADPH + H+
-
-
-
r
2-dehydropantoate + NADH + H+
-
736827
Thermococcus kodakarensis
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADH + H+
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
736827
Thermococcus kodakarensis
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADH + H+
-
736827
Thermococcus kodakarensis KUW1
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADH + H+
the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes
736827
Thermococcus kodakarensis KUW1
(R)-pantoate + NAD+
-
-
-
r
2-dehydropantoate + NADPH + H+
-
736827
Thermococcus kodakarensis
(R)-pantoate + NADP+
-
-
-
r
additional information
D-pantoate is much more preferred over L-pantoate in the reduction reaction, suggesting that the enzyme generates D-pantoate from 2-oxopantoate in the oxidation reaction
736827
Thermococcus kodakarensis
?
-
-
-
-
additional information
D-pantoate is much more preferred over L-pantoate in the reduction reaction, suggesting that the enzyme generates D-pantoate from 2-oxopantoate in the oxidation reaction
736827
Thermococcus kodakarensis KUW1
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
Thermococcus kodakarensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
90
-
recombinant enzyme
Thermococcus kodakarensis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
50
110
and above, activity range, profile overview
Thermococcus kodakarensis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
90
purified recombinant enzyme, pH 6.4, completely stable at for at least 24 h
Thermococcus kodakarensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.22
-
NADPH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
2.41
-
NAD+
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
3.17
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
3.8
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
19.7
-
NADH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
23.1
-
2-dehydropantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.4
-
recombinant enzyme
Thermococcus kodakarensis
General Information
General Information
Commentary
Organism
malfunction
gene disruption of gene TK1968results in a strain with growth defects that are complemented by addition of pantoate
Thermococcus kodakarensis
metabolism
ketopantoate reductase from the hyperthermophilic archaeon Thermococcus kodakarensis catalyses the second step in CoA biosynthesis, the reduction of 2-oxopantoate to pantoate. CoA biosynthesis in the archaeon is regulated by feedback inhibition of enzyme ketopantoate reductase
Thermococcus kodakarensis
General Information (protein specific)
General Information
Commentary
Organism
malfunction
gene disruption of gene TK1968results in a strain with growth defects that are complemented by addition of pantoate
Thermococcus kodakarensis
metabolism
ketopantoate reductase from the hyperthermophilic archaeon Thermococcus kodakarensis catalyses the second step in CoA biosynthesis, the reduction of 2-oxopantoate to pantoate. CoA biosynthesis in the archaeon is regulated by feedback inhibition of enzyme ketopantoate reductase
Thermococcus kodakarensis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
29
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
60
-
NAD+
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
2220
-
NADPH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
3830
-
2-dehydropantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
6540
-
NADH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
29
-
(R)-pantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
60
-
NAD+
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
2220
-
NADPH
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
3830
-
2-dehydropantoate
recombinant enzyme, pH 6.4, 70°C
Thermococcus kodakarensis
6540
-
NADH
recombinant enzyme, pH 6.4, 70°C
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
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)
725293
Miller
PanG, a new ketopantoate reduc ...
Francisella tularensis subsp. novicida
J. Bacteriol.
195
965-976
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
736827
Tomita
Identification and characteriz ...
Thermococcus kodakarensis, Thermococcus kodakarensis KUW1
Mol. Microbiol.
90
307-321
2013
-
-
1
-
1
-
1
7
-
-
2
4
-
8
-
-
1
-
-
-
-
-
13
1
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
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684140
Ciulli
pH-tuneable binding of 2-phosp ...
Escherichia coli
Acta Crystallogr. Sect. D
63
171-178
2007
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
687675
Ciulli
Crystal structure of Escherich ...
Escherichia coli
J. Biol. Chem.
282
8487-8497
2007
-
-
1
1
6
-
-
3
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
2
1
-
-
2
-
-
-
-
-
1
2
1
6
-
-
-
-
3
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
669806
Ciulli
Probing hot spots at protein-l ...
Escherichia coli
J. Med. Chem.
49
4992-5000
2006
-
-
-
-
-
-
7
1
-
-
-
1
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
3
6
-
-
-
-
-
3
-
-
-
-
7
6
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
667561
Ciulli
Biophysical tools to monitor e ...
Escherichia coli
Biochem. Soc. Trans.
33
767-771
2005
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667687
Lobley
The crystal structure of Esche ...
Escherichia coli
Biochemistry
44
8930-8939
2005
-
-
1
1
7
-
-
1
-
-
-
1
-
2
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
7
-
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654677
Zheng
Substrate specificity and kine ...
Escherichia coli
Biochemistry
42
11289-11296
2003
-
-
1
-
-
-
-
8
-
-
-
1
-
2
-
-
-
-
-
-
-
-
7
-
1
-
-
-
1
1
-
4
-
-
-
-
-
1
4
-
-
-
-
-
-
8
-
-
-
1
-
-
-
-
-
-
-
-
7
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
656330
Merkamm
Ketopantoate reductase activit ...
Corynebacterium glutamicum
J. Biotechnol.
104
253-260
2003
-
-
1
-
-
-
-
1
-
-
-
1
-
3
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286110
Matak-Vinkovic
Crystal structure of Escherich ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia 845
Biochemistry
40
14493-14500
2001
-
-
1
1
1
-
-
4
-
2
4
2
-
7
-
1
1
-
-
-
2
-
4
3
-
-
-
2
-
-
-
3
-
-
-
-
-
1
3
1
1
-
-
-
-
4
-
2
4
2
-
-
1
1
-
-
2
-
4
3
-
-
-
2
-
-
-
-
-
-
-
-
-
-
286108
Zheng
Kinetic and mechanistic analys ...
Escherichia coli
Biochemistry
39
3708-3717
2000
-
-
1
-
-
-
2
4
-
1
4
1
-
2
-
-
1
-
-
-
1
-
2
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
2
-
4
-
1
4
1
-
-
-
1
-
-
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286109
Zheng
Identification of active site ...
Escherichia coli
Biochemistry
39
16244-16251
2000
5
-
1
-
10
-
-
12
-
1
1
-
-
2
-
-
1
-
-
-
1
-
2
1
-
-
-
-
1
-
-
2
-
-
-
5
-
1
2
-
10
-
-
-
-
12
-
1
1
-
-
-
-
1
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286106
Elischewski
Pantothenate production in Esc ...
Escherichia coli
J. Biotechnol.
75
135-146
1999
-
-
1
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286107
Frodyma
ApbA, the ketopantoate reducta ...
Escherichia coli, Escherichia coli BL21/lambdaDE3, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium, Stenotrophomonas maltophilia 845, Stenotrophomonas maltophilia
J. Biol. Chem.
273
5572-5576
1998
-
-
1
-
-
-
-
2
-
-
1
3
-
10
-
-
1
-
-
-
6
-
12
2
1
-
-
-
1
-
-
8
-
-
-
-
-
1
8
-
-
-
-
-
-
2
-
-
1
3
-
-
-
1
-
-
6
-
12
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
286102
Kataoka
-
Novel enzymic production of D- ...
Agrobacterium sp., Agrobacterium tumefaciens, Pseudomonas putida, Stenotrophomonas maltophilia
Agric. Biol. Chem.
54
177-182
1990
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
286103
Shimizu
Ketopantoic acid reductase of ...
Saccharomyces cerevisiae, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia 845
J. Biol. Chem.
263
12077-12084
1988
-
-
-
1
-
-
10
4
-
1
4
-
-
6
-
-
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 ...
Escherichia coli, Saccharomyces cerevisiae
J. Biol. Chem.
250
2311-2314
1975
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286104
King
-
Separation and preliminary stu ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae NRRL Y-2034
J. Biol. Chem.
247
4096-4098
1972
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
2
-
4
-
-
-
-
-
2
1
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
4
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-