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Synonyms
ketopantoate reductase, 2-dehydropantoate 2-reductase, tk-kpr, kpa reductase, ketopantoic acid reductase, conjugated polyketone reductase, tk1968, 2-ketopantoate reductase, tk1968 protein,
more
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2-dehydropantoate + NADPH
(R)-pantoate + NADP+
ketopantoate + NADPH
pantoate + NADP+
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
-
-
-
?
2-oxoisovalerate + NADPH
2-hydroxyvalerate + NADP+
-
low activity
-
-
r
2-oxopantoate + 3'-NADPH
(R)-pantoate + 3'-NADP+
-
-
-
-
r
2-oxopantoate + alpha-NADPH
(R)-pantoate + alpha-NADP+
-
-
-
-
r
2-oxopantoate + beta-NADPH
(R)-pantoate + beta-NADP+
-
highly specific for
-
-
r
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
part of the pantothenate biosynthesis
-
-
?
2-oxopantoate + thio-NADPH
(R)-pantoate + thio-NADP+
-
-
-
-
r
3-methyl-2-oxo-n-valerate + NADPH
2-hydroxy-3-methyl-n-valerate + NADP+
-
low activity
-
-
r
alpha-ketopantoate + NADPH
D-pantoate + NADP+
ketopantoate + ?
pantothenate + ?
-
-
-
?
ketopantoate + NADPH
pantoate + NADP+
ketopantoic acid + NADPH
pantoic acid + NADP+
additional information
?
-
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
-
-
-
?
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
an essential step for the biosynthesis of pantothenate, i.e. vitamin B5
-
-
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5
-
-
?
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
substrate and product binding structures, hinge bending between the N- and C-terminal domains is observed, which triggers the switch of the essential Lys176 to form a key hydrogen bond with the C2 hydroxyl of pantoate, pantoate forms additional interactions with conserved residues Ser244, Asn98, and Asn180 and with two conservatively varied residues, Asn194 and Asn241, overview
-
-
r
ketopantoate + NADPH
pantoate + NADP+
pantothenate biosynthetic pathway
-
?
ketopantoate + NADPH
pantoate + NADP+
the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
-
-
r
ketopantoate + NADPH
pantoate + NADP+
substrate binding structure and thermodynamics
-
-
r
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
-
-
r
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
B-specific
-
r
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
pantothenate/coenzyme A biosynthetic pathway
-
r
ketopantoate + NADPH
pantoate + NADP+
-
-
-
?
ketopantoate + NADPH
pantoate + NADP+
-
-
-
-
r
ketopantoate + NADPH
pantoate + NADP+
-
the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
-
-
r
ketopantoate + NADPH
pantoate + NADP+
-
the 4-proS hydrogen is transferred from NADPH to ketopantoate to form pantoate and NADP+, ligand binding analysis by NMR spectroscopy
-
-
r
ketopantoic acid + NADPH
pantoic acid + NADP+
-
-
-
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
B-specific
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview
-
-
?
additional information
?
-
-
complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview
-
-
?
additional information
?
-
conformational changes can occur upon substrate binding in the hinge region leading to partial closure of the cleft between the domains. Such motions may be present to some degree in the apo form
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity for double mutant K176A/E256A
-
-
?
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2-dehydropantoate + NADPH
(R)-pantoate + NADP+
ketopantoate + NADPH
pantoate + NADP+
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
-
-
-
?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
part of the pantothenate biosynthesis
-
-
?
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
pantothenate/coenzyme A biosynthetic pathway
-
r
ketopantoate + NADPH
pantoate + NADP+
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
an essential step for the biosynthesis of pantothenate, i.e. vitamin B5
-
-
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5
-
-
?
ketopantoate + NADPH
pantoate + NADP+
pantothenate biosynthetic pathway
-
?
ketopantoate + NADPH
pantoate + NADP+
the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
-
-
r
ketopantoate + NADPH
pantoate + NADP+
-
-
-
?
ketopantoate + NADPH
pantoate + NADP+
-
the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
-
-
r
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0.03
2-dehydropantoate
pH 7.5, 27°C, wild-type enzyme
8.7
2-oxoisovalerate
-
pH 7.5, 25°C, recombinant enzyme
0.12
2-oxopantoate
-
pH 7.5, 25°C, recombinant enzyme
0.075
3'-NADPH
-
pH 7.5, 25°C, recombinant enzyme
3.8
3-methyl-2-oxo-n-valerate
-
pH 7.5, 25°C, recombinant enzyme
0.036
alpha-NADPH
-
pH 7.5, 25°C, recombinant enzyme
0.004
beta-NADPH
-
pH 7.5, 25°C, recombinant enzyme
0.018
thio-NADPH
-
pH 7.5, 25°C, recombinant enzyme
additional information
additional information
-
0.06
ketopantoate
-
0.004
NADPH
-
0.007
NADPH
pH 7.5, 27°C, wild-type enzyme
0.038
ketopantoate
-
+/-0.009, mutant K176C, alkylated
0.07
ketopantoate
-
+/-0.01, mutant K176C
0.12
ketopantoate
-
+/-0.008
0.95
ketopantoate
-
+/-0.29, mutant E256D
7.5
ketopantoate
-
+/-2.9, mutant K256A
40
ketopantoate
-
+/-6, mutant K176A
0.002
NADPH
-
+/-0.0003, mutant E256A
0.0029
NADPH
-
+/-0.0006, mutant E256D
0.0038
NADPH
-
+/-0.0003, mutant K176C, alkylated
0.0066
NADPH
-
+/-0.0016, mutant K176C
0.016
NADPH
-
+/-0.003, mutant K176A
additional information
additional information
kinetics and thermodynamics, wild-type enzyme, overview
-
additional information
additional information
-
kinetics and thermodynamics, wild-type enzyme, overview
-
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics, pH-dependence of kinetics with different substrates, overview
-
additional information
additional information
-
kinetics and thermodynamics, overview
-
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prismic crystals, hanging drop vapor-diffusion technique
purified enzyme with bound NADP+, hanging drop vapour diffusion method, 10-15 mg/ml protein at 4°C is mixed with ketopantoate and NADP+ in a ratio of 5:1 and 2:1, respectively, in 0.1 M sodium acetate, pH 4.0-5.0, with 10%2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.1 A resolution, ternary complex modelling
purified recombinant His6-tagged enzyme in complex with 2'-monophosphoadenosine 5'-diphosphoribose, 4°C, 10-15 mg/ml protein with NADPH and pantoate at a final ligand:protein ratio of 2:1 and 5:1, respectively, mixing with 10% 2-methyl-2,4-pentanediol buffered with 0.1 M sodium acetate pH 4.0-5.0, X-ray diffraction structure determination and analysis at 1.95-2.0 A resolution
purified recombinant His6-tagged enzyme in complex with NADP+ and pantoate, hanging drop vapor-diffusion technique, 20°C, 15-30 mg/ml protein with 2 mM NADP+ and 10 mM pantoate, 0.002 ml of protein solution is mixed with an equal volume of well solution containing 35% v/v dioxane, cryoprotection with 20% v/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.3 A resolution
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D248A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
E210A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
R31A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
D248A
-
site-directed mutagenesis, wild-type activity
E210A
-
site-directed mutagenesis, wild-type activity
E240A
-
site-directed mutagenesis, wild-type activity
E256A
-
site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme
E256D
-
wild-type activity
K176A
-
site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme
K176A/E256A
-
double mutant, no activity
K176C
-
wild-type activity
K72A
-
site-directed mutagenesis, wild-type activity
E256A
site-directed mutagenesis, nearly inactive mutant, 2600fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain
E256A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
K176A
site-directed mutagenesis, nearly inactive mutant, 78000fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain
K176A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
K72A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
K72A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
N98A
site-directed mutagenesis, nearly inactive mutant, 4000fold reduced catalytic efficiency, no complementation of a panE knockout mutant strain
N98A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
S244A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain
S244A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
additional information
Lys176 and Glu256 important for binding ketopantoate and the catalytic mechanism
additional information
-
Lys176 and Glu256 important for binding ketopantoate and the catalytic mechanism
additional information
-
Lys176 acts as general acid in ketopantoate reduction and is involved in catalysis and ketopantoate binding, E256A functions in D-pantoate and ketopantoate binding in ketopantoate reductase
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Wilken, D.R.; King, H.L.; Dyar, R.E.
Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate
J. Biol. Chem.
250
2311-2314
1975
Saccharomyces cerevisiae, Escherichia coli
brenda
Elischewski, F.; Puhler, A.; Kalinowski, J.
Pantothenate production in Escherichia coli K12 by enhanced expression of the panE gene encoding ketopantoate reductase
J. Biotechnol.
75
135-146
1999
Escherichia coli
brenda
Frodyma, M.E.; Downs, D.
ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway
J. Biol. Chem.
273
5572-5576
1998
Escherichia coli, Escherichia coli BL21/lambdaDE3, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia 845
brenda
Zheng, R.; Blanchard, J.S.
Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase
Biochemistry
39
3708-3717
2000
Escherichia coli
brenda
Zheng, R.; Blanchard, J.S.
Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue
Biochemistry
39
16244-16251
2000
Escherichia coli
brenda
Matak-Vinkovic, D.; Vinkovic, M.; Saldanha, S.A.; Ashurst, J.L.; von Delft, F.; Inoue, T.; Miguel, R.N.; Smith, A.G.; Blundell, T.L.; Abell, C.
Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism
Biochemistry
40
14493-14500
2001
Escherichia coli (P0A9J4), Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia 845
brenda
Zheng, R.; Blanchard, J.S.
Substrate specificity and kinetic isotope effect analysis of the Eschericia coli ketopantoate reductase
Biochemistry
42
11289-11296
2003
Escherichia coli
brenda
Ciulli, A.; Abell, C.
Biophysical tools to monitor enzyme-ligand interactions of enzymes involved in vitamin biosynthesis
Biochem. Soc. Trans.
33
767-771
2005
Escherichia coli
brenda
Lobley, C.M.; Ciulli, A.; Whitney, H.M.; Williams, G.; Smith, A.G.; Abell, C.; Blundell, T.L.
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound
Biochemistry
44
8930-8939
2005
Escherichia coli (P0A9J4), Escherichia coli
brenda
Ciulli, A.; Williams, G.; Smith, A.G.; Blundell, T.L.; Abell, C.
Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods
J. Med. Chem.
49
4992-5000
2006
Escherichia coli
brenda
Ciulli, A.; Lobley, C.M.; Tuck, K.L.; Smith, A.G.; Blundell, T.L.; Abell, C.
pH-tuneable binding of 2-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study
Acta Crystallogr. Sect. D
63
171-178
2007
Escherichia coli (P0A9J4), Escherichia coli
brenda
Ciulli, A.; Chirgadze, D.Y.; Smith, A.G.; Blundell, T.L.; Abell, C.
Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity
J. Biol. Chem.
282
8487-8497
2007
Escherichia coli (P0A9J4), Escherichia coli
brenda
Headey, S.J.; Vom, A.; Simpson, J.S.; Scanlon, M.J.
Backbone assignments of the 34 kDa ketopantoate reductase from E. coli
Biomol. NMR Assign.
2
93-96
2008
Escherichia coli (P0A9J4)
brenda
Zhang, B.; Zhang, X.M.; Wang, W.; Liu, Z.Q.; Zheng, Y.G.
Metabolic engineering of Escherichia coli for D-pantothenic acid production
Food Chem.
294
267-275
2019
Escherichia coli, Escherichia coli W3110
brenda