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Information on EC 1.1.1.169 - 2-dehydropantoate 2-reductase
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EC Tree
1.1.1.169 2-dehydropantoate 2-reductaseSpecify your search results
Word Map
- 1.1.1.169
- pantothenate
-
nadph-dependent
-
pane
- hydroxymethyltransferase
-
ketopantoyl
- 2'-phosphate
-
fragment-based
- d-2-hydroxyacid
-
parapsilosis
- kodakarensis
The enzyme appears in viruses and cellular organisms
Synonyms
ketopantoate reductase, 2-dehydropantoate 2-reductase, tk-kpr, kpa reductase, ketopantoic acid reductase, conjugated polyketone reductase, tk1968, 2-ketopantoate reductase, tk1968 protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-dehydropantoate 2-reductase
2-ketopantoate reductase
2-ketopantoic acid reductase
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2-oxopantoate reductase
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conjugated polyketone reductase
CPR
ketopantoate reductase
ketopantoic acid reductase
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KPA reductase
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KPR
PanE
Tk-KPR
TK1968
TK1968 protein
additional information
2-ketopantoate reductase
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ketopantoate reductase
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KPR
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additional information
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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+
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(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
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(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
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redox reaction
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-pantoate + NAD+
2-dehydropantoate + NADH + H+
low activity
-
-
r
(S)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
low activity
-
-
r
2-oxopantoate + beta-NADPH
(R)-pantoate + beta-NADP+
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highly specific for
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r
3-methyl-2-oxo-n-valerate + NADPH
2-hydroxy-3-methyl-n-valerate + NADP+
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low activity
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-
r
ketopantoic acid + NADH
pantoic acid + NAD+
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-
-
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
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?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
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-
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?
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
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-
-
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
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-
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r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
substrate binding structure analysis, overview
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r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
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-
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r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
substrate binding structure analysis, overview
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r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
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-
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r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
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
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r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
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-
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r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
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
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r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
an essential step for the biosynthesis of pantothenate, i.e. vitamin B5
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r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5
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-
?
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
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r
2-keto-3-hydroxyisovalerate + NADPH
? + NADP+
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r
2-oxopantoate + NADPH
(R)-pantoate + NADP+
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reaction is part of the D-pantothenate biosynthesis
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?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
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part of the pantothenate biosynthesis
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?
alpha-ketopantoate + NADPH
D-pantoate + NADP+
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pantothenate/coenzyme A biosynthetic pathway
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r
ketopantoate + NADPH
pantoate + NADP+
pantothenate biosynthetic pathway
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?
ketopantoate + NADPH
pantoate + NADP+
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the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
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r
ketopantoate + NADPH
pantoate + NADP+
the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA
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r
ketopantoate + NADPH
pantoate + NADP+
substrate binding structure and thermodynamics
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r
ketopantoate + NADPH
pantoate + NADP+
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the 4-proS hydrogen is transferred from NADPH to ketopantoate to form pantoate and NADP+, ligand binding analysis by NMR spectroscopy
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r
ketopantoate + NADPH
pantoate + NADP+
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?
ketopantoate + NADPH
pantoate + NADP+
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thiamine synthesis, pantothenate and thiamine biosynthetic pathway
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?
ketopantoic acid + NADPH
D-pantoic acid + NADP+
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r
ketopantoic acid + NADPH
pantoic acid + NADP+
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B-specific
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?
ketopantoic acid + NADPH
pantoic acid + NADP+
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?
ketopantoic acid + NADPH
pantoic acid + NADP+
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?
additional information
?
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no activity for double mutant K176A/E256A
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?
additional information
?
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complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview
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?
additional information
?
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complex formation of 2'-monophosphoadenosine 5'-diphosphoribose upon incubation of NADPH at pH 5.0, structure analysis, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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no activity with pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvic acid, alpha-ketoglutarate, alpha-ketobutyrate, acetaldehyde at 0.5 mM
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?
additional information
?
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3.8-fold higher specific activity with NADPH than with NADH
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?
additional information
?
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high specificity, among a variety of carbonyl compounds only ketopantoic acid and 2-keto-3-hydroxyisovalerate can serve as substrate
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?
additional information
?
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high specificity, among a variety of carbonyl compounds only ketopantoic acid and 2-keto-3-hydroxyisovalerate can serve as substrate
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-ketopantoate + NADPH
D-pantoate + NADP+
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pantothenate/coenzyme A biosynthetic pathway
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r
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
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-
-
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
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-
-
?
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
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-
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r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
-
-
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r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
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-
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r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
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
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
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
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-oxopantoate + NADPH
(R)-pantoate + NADP+
-
reaction is part of the D-pantothenate biosynthesis
-
-
?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
part of the pantothenate biosynthesis
-
-
?
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+
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+
-
thiamine synthesis, pantothenate and thiamine biosynthetic pathway
-
?
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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
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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
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noncompetitive with ketopantoic acid at saturation level of NADPH, noncompetitive with NADPH at unsaturation level of ketopantoic acid
p-chloromercuribenzoate
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sulfhydryl reagents, slightly inhibitory
CoA
strong inhibition, competitive versus NADH, effect on enzyme kinetics, overview