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Information on EC 1.1.1.169 - 2-dehydropantoate 2-reductase
for references in articles please use BRENDA:EC1.1.1.169
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.169 2-dehydropantoate 2-reductase
The enzyme appears in viruses and cellular organisms
- 1.1.1.169
- pantothenate
-
nadph-dependent
-
pane
- hydroxymethyltransferase
-
ketopantoyl
- 2'-phosphate
-
fragment-based
- d-2-hydroxyacid
-
parapsilosis
- kodakarensis
showSynonyms
ketopantoate reductase, 2-dehydropantoate 2-reductase, kpa reductase, ketopantoic acid reductase, tk-kpr, conjugated polyketone reductase, tk1968 protein, tk1968, 2-ketopantoate reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-dehydropantoate 2-reductase
2-ketopantoate reductase
2-ketopantoic acid reductase
-
-
-
-
2-oxopantoate reductase
-
-
-
-
conjugated polyketone reductase
CPR
ketopantoate reductase
ketopantoic acid reductase
-
-
-
-
KPA reductase
-
-
-
-
KPR
PanE
Tk-KPR
TK1968
TK1968 protein
additional information
2-ketopantoate reductase
-
-
-
-
ketopantoate reductase
-
-
-
-
KPR
-
-
-
-
additional information
-
gene ilvC encodes a acetohydroxyacid isomeroreductase which also shows 2-hydropantoate 2-reductase activity
additional information
KPR belongs to the 6-phosphogluconate dehydrogenase superfamily in the SCOP database
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+
-
-
-
-
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+
molecular catalytic mechanism, substrate and cofactor binding, Asn98, Glu256, and Lys176 are essential, overview
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+
protein-ligand interactions, overview
-
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+
the enzyme follows a random addition mechanism in which the initial binding of NADPH is the kinetically preferred path, with a small degree of cooperativity between subunits. The mechanism of Staphylococcus aureus KPR is distinct from those of previously described members of the family of 2-hydroxyacid dehydrogenases
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
phosphopantothenate biosynthesis I, phosphopantothenate biosynthesis III (archaea)
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SYSTEMATIC NAME
IUBMB Comments
(R)-pantoate:NADP+ 2-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37211-74-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-pantoate + NAD+
2-dehydropantoate + NADH + H+
Substrates: low activity
Products: -
Products: -
r
(S)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: low activity
Products: -
Products: -
r
2-oxoisovalerate + NADPH
2-hydroxyvalerate + NADP+
-
Substrates: low activity
Products: -
Products: -
r
2-oxopantoate + 3'-NADPH
(R)-pantoate + 3'-NADP+
-
Substrates: -
Products: -
Products: -
r
2-oxopantoate + alpha-NADPH
(R)-pantoate + alpha-NADP+
-
Substrates: -
Products: -
Products: -
r
2-oxopantoate + beta-NADPH
(R)-pantoate + beta-NADP+
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Substrates: highly specific for
Products: -
Products: -
r
2-oxopantoate + thio-NADPH
(R)-pantoate + thio-NADP+
-
Substrates: -
Products: -
Products: -
r
3-methyl-2-oxo-n-valerate + NADPH
2-hydroxy-3-methyl-n-valerate + NADP+
-
Substrates: low activity
Products: -
Products: -
r
ketopantoic acid + NADH
pantoic acid + NAD+
-
Substrates: -
Products: -
Products: -
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: substrate binding structure analysis, overview
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: substrate binding structure analysis, overview
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: -
Products: -
Products: -
r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: 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
Products: -
Products: -
r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: -
Products: -
Products: -
r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: 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
Products: -
Products: -
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: an essential step for the biosynthesis of pantothenate, i.e. vitamin B5
Products: -
Products: -
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5
Products: -
Products: -
?
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: 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
Products: -
Products: -
r
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
r
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
r
2-keto-3-hydroxyisovalerate + NADPH
? + NADP+
-
Substrates: -
Products: -
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r
2-keto-3-hydroxyisovalerate + NADPH
? + NADP+
-
Substrates: -
Products: -
Products: -
r
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
Substrates: reaction is part of the D-pantothenate biosynthesis
Products: -
Products: -
?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
Substrates: part of the pantothenate biosynthesis
Products: -
Products: -
?
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
Substrates: B-specific
Products: -
Products: -
r
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
Substrates: pantothenate/coenzyme A biosynthetic pathway
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
Substrates: pantothenate biosynthetic pathway
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
Substrates: the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
Substrates: substrate binding structure and thermodynamics
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: the 4-proS hydrogen is transferred from NADPH to ketopantoate to form pantoate and NADP+, ligand binding analysis by NMR spectroscopy
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: thiamine synthesis, pantothenate and thiamine biosynthetic pathway
Products: -
Products: -
?
ketopantoic acid + ?
D-pantoic acid
-
Substrates: -
Products: -
Products: -
?
ketopantoic acid + NADPH
D-pantoic acid + NADP+
-
Substrates: -
Products: -
Products: -
r
ketopantoic acid + NADPH
D-pantoic acid + NADP+
-
Substrates: -
Products: -
Products: -
r
ketopantoic acid + NADPH
pantoic acid + NADP+
-
Substrates: B-specific
Products: -
Products: -
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
Substrates: B-specific
Products: -
Products: -
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantolactone + NADPH + H+
D-(-)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantolactone + NADPH + H+
D-(-)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity for double mutant K176A/E256A
Products: -
Products: -
?
additional information
?
-
Substrates: complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with ketopantoic acid is 100%, with ketopantoyl lactone 6%, with oxoalacetic acid 4%, no activity with 2-ketoisovaleric acid, pyruvic acid, 3-hydroxypyruvic acid, 3-phosphohydroxypyruvic acid, 2-ketobutyric acid, 2-ketoglutaric acid, and acetaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity with ketopantoic acid is 100%, with ketopantoyl lactone 6%, with oxoalacetic acid 4%, no activity with 2-ketoisovaleric acid, pyruvic acid, 3-hydroxypyruvic acid, 3-phosphohydroxypyruvic acid, 2-ketobutyric acid, 2-ketoglutaric acid, and acetaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvic acid, alpha-ketoglutarate, alpha-ketobutyrate, acetaldehyde at 0.5 mM
Products: -
Products: -
?
additional information
?
-
-
Substrates: 3.8-fold higher specific activity with NADPH than with NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: high specificity, among a variety of carbonyl compounds only ketopantoic acid and 2-keto-3-hydroxyisovalerate can serve as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: high specificity, among a variety of carbonyl compounds only ketopantoic acid and 2-keto-3-hydroxyisovalerate can serve as substrate
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
Substrates: pantothenate/coenzyme A biosynthetic pathway
Products: -
Products: -
r
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
?
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
Substrates: -
Products: -
Products: -
r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: 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
Products: -
Products: -
r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: 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
Products: -
Products: -
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: an essential step for the biosynthesis of pantothenate, i.e. vitamin B5
Products: -
Products: -
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5
Products: -
Products: -
?
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
Substrates: reaction is part of the D-pantothenate biosynthesis
Products: -
Products: -
?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
Substrates: part of the pantothenate biosynthesis
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
Substrates: pantothenate biosynthetic pathway
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
Substrates: the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
Products: -
Products: -
r
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoate + NADPH
pantoate + NADP+
-
Substrates: thiamine synthesis, pantothenate and thiamine biosynthetic pathway
Products: -
Products: -
?
ketopantolactone + NADPH + H+
D-(-)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantolactone + NADPH + H+
D-(-)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
cofactor binding structure and thermodynamics, the cofactor is bound in the active site cleft between the N-terminal Rossmann-fold domain and the C-terminal alpha-helical domain
NADP+
dependent on, binding structure of 2'-monophosphoadenosine 5'-diphosphoribose, a fragment of NADP+ that lacks the nicotinamide ring, bound at the enzyme active site in the opposite orientation to that observed for NADP+, with the adenine ring occupying the lipophilic nicotinamide pocket, binding structure, overview
NADP+
the binding sites of CoA and NADP+ overlap, explaining the competitive manner of inhibition by CoA, binding structure analysis, overview
additional information
-
in presence of NADPH the ketopantoic acid reductase does not reduce artificial dye electron acceptors
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
does not require Mg2+, independent of divalent metal ions
additional information
does not require Mg2+, independent of divalent metal ions
additional information
-
does not require Mg2+, independent of divalent metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-pantoic acid
-
noncompetitive with ketopantoic acid at saturation level of NADPH, noncompetitive with NADPH at unsaturation level of ketopantoic acid
p-chloromercuribenzoate
-
sulfhydryl reagents, slightly inhibitory
CoA
strong inhibition, competitive versus NADH, effect on enzyme kinetics, overview
CoA
feedback inhibition, competitive with NADPH, the binding sites of CoA and NADP+ overlap, explaining the competitive manner of inhibition by CoA, binding structure analysis, overview
NADP+
-
competitive with NADPH at unsaturation level of ketopantoic acid
additional information
-
protein-ligand interaction determination and analysis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
formate
-
E256A mutant activity greatly increased, twice as high at pH 7.2 as at pH 5.9
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE