1.1.1.169: 2-dehydropantoate 2-reductase
This is an abbreviated version!
For detailed information about 2-dehydropantoate 2-reductase, go to the full flat file.
Word Map on EC 1.1.1.169
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1.1.1.169
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pantothenate
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nadph-dependent
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pane
-
hydroxymethyltransferase
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ketopantoyl
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2'-phosphate
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fragment-based
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d-2-hydroxyacid
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parapsilosis
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kodakarensis
- 1.1.1.169
- pantothenate
-
nadph-dependent
-
pane
- hydroxymethyltransferase
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ketopantoyl
- 2'-phosphate
-
fragment-based
- d-2-hydroxyacid
-
parapsilosis
- kodakarensis
Reaction
Synonyms
2-dehydropantoate 2-reductase, 2-ketopantoate reductase, 2-ketopantoic acid reductase, 2-oxopantoate reductase, conjugated polyketone reductase, CPR, ilvC, ketopantoate reductase, ketopantoic acid reductase, KPA reductase, KPR, More, PanE, panG, Tk-KPR, TK1968, TK1968 protein
ECTree
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Substrates Products
Substrates Products on EC 1.1.1.169 - 2-dehydropantoate 2-reductase
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REACTION DIAGRAM
(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+
-
highly specific for
-
-
r
3-methyl-2-oxo-n-valerate + NADPH
2-hydroxy-3-methyl-n-valerate + NADP+
-
low activity
-
-
r
ketopantoic acid + NADH
pantoic acid + NAD+
-
-
-
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
-
-
?
(R)-4-dehydropantoate + NADPH + H+
(R)-pantoate + NADP+
-
-
-
?
(R)-pantoate + NAD+
2-dehydropantoate + NADH + H+
-
-
-
r
2-dehydropantoate + NADPH + H+
-
-
-
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
substrate binding structure analysis, overview
-
-
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
-
-
-
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
substrate binding structure analysis, overview
-
-
r
(R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+
-
-
-
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+
-
-
-
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-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
2-keto-3-hydroxyisovalerate + NADPH
? + NADP+
-
-
-
r
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
-
-
?
alpha-ketopantoate + NADPH
D-pantoate + NADP+
-
pantothenate/coenzyme A biosynthetic pathway
-
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+
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
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
ketopantoate + NADPH
pantoate + NADP+
-
-
-
?
ketopantoate + NADPH
pantoate + NADP+
-
thiamine synthesis, pantothenate and thiamine biosynthetic pathway
-
?
ketopantoic acid + NADPH
D-pantoic acid + NADP+
-
-
-
r
ketopantoic acid + NADPH
pantoic acid + NADP+
-
B-specific
-
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
-
-
?
ketopantoic acid + NADPH
pantoic acid + NADP+
-
-
-
?
additional information
?
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-
no activity for double mutant K176A/E256A
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvic acid, alpha-ketoglutarate, alpha-ketobutyrate, acetaldehyde at 0.5 mM
-
-
?
additional information
?
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-
3.8-fold higher specific activity with NADPH than with NADH
-
-
?
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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-
?