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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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 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, ketopantoic acid reductase, tk-kpr, kpa reductase, conjugated polyketone reductase, tk1968, 2-ketopantoate reductase, tk1968 protein, 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: -
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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: -
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r
2-oxopantoate + alpha-NADPH
(R)-pantoate + alpha-NADP+
-
Substrates: -
Products: -
Products: -
r
2-oxopantoate + beta-NADPH
(R)-pantoate + beta-NADP+
-
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: -
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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: -
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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
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: -
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r
2-dehydropantoate + NADH + H+
(R)-pantoate + NAD+
Substrates: -
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: an essential step for the biosynthesis of pantothenate, i.e. vitamin B5
Products: -
Products: -
r
2-dehydropantoate + NADPH
(R)-pantoate + NADP+
Substrates: -
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: -
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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: reaction is part of the D-pantothenate biosynthesis
Products: -
Products: -
?
2-oxopantoate + NADPH
(R)-pantoate + NADP+
-
Substrates: -
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: -
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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: 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 4-proS hydrogen is transferred from NADPH to ketopantoate to form pantoate and NADP+, ligand binding analysis by NMR spectroscopy
Products: -
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r
ketopantoate + NADPH
pantoate + NADP+
Substrates: substrate binding structure and thermodynamics
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: -
?
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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: the enzyme is involved in the biosynthesis of pantothenate, i.e. vitamin B5
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 + 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: 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
0.0096
(R)-4-dehydropantoate
wild type enzyme, at pH 7.5 and 25°C
8.1
(R)-4-dehydropantoate
mutant enzyme A181L, at pH 7.5 and 25°C
additional information
additional information
-
steady-state kinetics, pH-dependence of kinetics with different substrates, overview
-
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 and thermodynamics, 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
Michaelis-Menten kinetics in both reaction directions
-
additional information
additional information
-
Michaelis-Menten kinetics in both reaction directions
-
additional information
additional information
the enzyme shows strong positive cooperativity in kinetics. 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
-
additional information
additional information
-
the enzyme shows strong positive cooperativity in kinetics. 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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.6
(R)-4-dehydropantoate
wild type enzyme, at pH 7.5 and 25°C
18.2
(R)-4-dehydropantoate
mutant enzyme A181L, at pH 7.5 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
(R)-4-dehydropantoate
wild type enzyme, at pH 7.5 and 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0246
-
recombinant Escherichia coli mutant strain expresing the enzyme
16
-
optimal reaction conditions using NADPH
61
-
optimal reaction conditions using NADH
additional information
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
-
3.8-fold higher specific activity with NADPH than with NADH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
-
reduction of pantoic acid at 42°C
6.4
7.5
additional information
-
activity decreases with pH increase, reduction of ketopantoic acid
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3 - 6.5
-
pH 4.3: about 10% of activity maximum, pH 6.5: about 40% of activity maximum
additional information
-
pH-dependence of kinetics with different substrates, modeling, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
35 - 40
42
-
reduction of ketopantoic acid at pH 6.0
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 60
-
15°C: about 70% of activity maximum, 60°C: about 85% of activity maximum
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ilvC, the enzyme activity in the organism is only encoded by ilvC, a bifunctional enzyme showing acetohydroxyacid isomeroreductase and 2-hydropantoate 2-reductase activity
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the family of 2-hydroxyacid dehydrogenases
malfunction
metabolism
physiological function
additional information
malfunction
-
both the homologous gene from Enterococcus faecalis V583 (EF1861) and Escherichia coli panE functionally complement Francisella novicida lacking any KPR. Furthermore, panG from Francisella novicida can complement an Escherichia coli KPR double mutant. A panG deletion mutant is a pantothenate auxotroph and is genetically and chemically complemented with pang in trans or with the addition of pantolactone
malfunction
gene disruption of gene TK1968results in a strain with growth defects that are complemented by addition of pantoate
malfunction
enzyme mutation A181L causes substitution of Ser239 and increases the Km for ketopantoate 844fold, without affecting kcat. The decrease in 2-dehydropantoate affinity enhances the already kinetically preferred NADPH binding path, making the random mechanism appear to be sequentially ordered and reducing the kinetic cooperativity
malfunction
-
gene disruption of gene TK1968results in a strain with growth defects that are complemented by addition of pantoate
-
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
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
-
physiological function
ketopantoate reductase catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate which is a step in the biosynthesis of coenzyme A
physiological function
ketopantoate reductase (KPR) catalyzes the NADPH-dependent production of pantoate, an essential precursor in the biosynthesis of coenzyme A
physiological function
ketopantoate reductase (KPR) catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate to pantoate, and is a target of the feedback inhibition by CoA in archaea. Coenzyme A (CoA) plays essential roles in a variety of metabolic pathways in all three domains of life. The biosynthesis pathway of CoA is strictly regulated by feedback inhibition. In bacteria and eukaryotes, pantothenate kinase is the target of feedback inhibition by CoA
physiological function
-
ketopantoate reductase catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate which is a step in the biosynthesis of coenzyme A
-
physiological function
-
ketopantoate reductase (KPR) catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate to pantoate, and is a target of the feedback inhibition by CoA in archaea. Coenzyme A (CoA) plays essential roles in a variety of metabolic pathways in all three domains of life. The biosynthesis pathway of CoA is strictly regulated by feedback inhibition. In bacteria and eukaryotes, pantothenate kinase is the target of feedback inhibition by CoA
-
additional information
residue Ser239 is known to be important for the binding affinity of 2-dehydropantoate
additional information
-
residue Ser239 is known to be important for the binding affinity of 2-dehydropantoate
additional information
CoA and 2-oxopantoate cooperatively trigger a conformational change from an open form to a closed enzyme form, structure analysis, overview
additional information
-
CoA and 2-oxopantoate cooperatively trigger a conformational change from an open form to a closed enzyme form, structure analysis, overview
additional information
-
CoA and 2-oxopantoate cooperatively trigger a conformational change from an open form to a closed enzyme form, structure analysis, overview
-
Show AA Sequence and Transmembrane Helices (22072 entries)
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Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31100
33000
33866
-
1 * 33000 gel filtration, 1 * 33866 elelectrospray mass spectrometry analysis, 1 * 33870 amino acid sequence
33870
-
1 * 33000 gel filtration, 1 * 33866 elelectrospray mass spectrometry analysis, 1 * 33870 amino acid sequence
34000
34048
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
31100
-
1 * 31100, HPLC gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
oligomer
additional information
homodimer
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE
-
monomer
-
1 * 33000 gel filtration, 1 * 33866 elelectrospray mass spectrometry analysis, 1 * 33870 amino acid sequence
monomer
-
1 * 31100, HPLC gel filtration
additional information
homology modeling of structure of the ternary KPR complex using the crystal structure of Staphylococcus aureus apo-KPR as a search model, PDB ID 3G17
additional information
-
homology modeling of structure of the ternary KPR complex using the crystal structure of Staphylococcus aureus apo-KPR as a search model, PDB ID 3G17
additional information
enzyme structure analysis and comparisons, overview
additional information
-
enzyme structure analysis and comparisons, overview
additional information
-
enzyme structure analysis and comparisons, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
purified recombinant wild-type and mutant A181L enzymes, sitting drop vapor diffusion , for the wild-type enzyme complexed with 2-dehydropantoateand NADP+: mixing of 0.001 ml of 10 mg/mL protein in 4 mM 2-dehydropantoate, 4 mM NADP+, 50 mM NaCl, and 25 mM Tris, pH 8.0 with 0.001 ml of reservoir solution containing 300 mM magnesium acetate, 100 mM MES buffer, pH 6.6, and 15% PEG 3350, 2-3 days, 20°C, for the mutant enzyme A181L complexed with NADP+: mixing of 0.001ml of 10 mg/mL protein in 4 mM NADP+, 50 mM NaCl, and 25 mM Tris, pH 8.0, with 0.001 ml of the reservoir solution containing 6% tacsimate, 100 mM MES, pH 6, and 15% PEG 3350, 2-3 days, 20°C, X-ray diffraction structure determination and analysis at 1.81 and 2.62 A resolution, respectively
sitting drop vapor diffusion method, using 300 mM magnesium acetate, 100 mM MES buffer (pH 6.6), and 15% (w/v) polyethylene glycol 3350
purified enzyme in complex with CoA and 2-oxopantoate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein and 1 mM CoA and 1 mM 2-oxopantoate with 0.001 ml of reservoir solution containing 100 mM Na acetate, pH 4.5, 20-25% v/v 2-methyl-2,4-pentanediol, and equilibration against 0.5 ml of reservoir solution, at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.65 A resolution, modeling by molecular replacement method using N-terminal (1-165 residues) and C-terminal (171-309 residues) domains of Ec-KPR structure, PDB ID 2OFP, as separated search models, respectively
purified recombinant tagged enzyme mutant C84A, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg /ml protein in 10 mM Tris-HCl, pH 8.0, 1 mM dithiothreitol, mM NADH, and 1 mM 2-oxopantoate, with 0.001 ml of reservoir solution containing 100 mM sodium acetate, pH 5.5, 10% w/v PEG 3350, 20% v/v 2-propanol, and equilibration against 0.5 ml reservoir solution, at 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method for modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D248A
E210A
E256A
K176A
K72A
N98A
R31A
site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview
S244A
A181L
C84A
C84A
additional information
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
E256A
-
site-directed mutagenesis, significant reduction in catalytic efficiency of enzyme
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, significant reduction in catalytic efficiency of enzyme
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
A181L
site-directed mutagenesis, the substitution displaces Ser239 and increases the Km for ketopantoate 844fold, without affecting kcat. The decrease in 2-dehydropantoate affinity enhances the already kinetically preferred NADPH binding path, making the random mechanism appear to be sequentially ordered and reducing the kinetic cooperativity
A181L
the substitution increases the Km of ketopantoate 844fold, without affecting the kcat value
C84A
site-directed mutagenesis, crystal structure analysis, overview
C84A
-
site-directed mutagenesis, crystal structure analysis, overview
-
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
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
generation of a gene TK1968 disruption mutant
additional information
-
generation of a gene TK1968 disruption mutant
additional information
-
generation of a gene TK1968 disruption mutant
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 90
purified recombinant enzyme, pH 6.4, completely stable at for at least 24 h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.01 M Tris/HCl buffer, pH 7.4, 0.1 mM DTT, 0.2 M NaCl, 6 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel chromatography
native wild-type enzyme by anion exchange and adsorption chromatography, and gel filtration, recombinant His6-tagged enzyme by nickel affinity chromatography
on nickel-nitrilotriacetic acid resin and by gel filtration, more than 98% pure
recombinant C-terminally His-tagged wild-type and mutant enzymes
recombinant enzyme from Escherichia coli by heat treatment, anion-exchange chromatography, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain Rosetta2 (DE3) pLysS by nickel affinity chromatography, avidin affinity chromatography, and dialysis
recombinant wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer from Escherichia coli by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expressed with glucose dehydrogenase from Bacillus subtilis in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli BL21/lambdaDE3
-
gene ilvC, complementation of an enzyme-deficient Escherichia coli mutant strain
-
gene TK1968, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli
gene TK1968, recombinant coexpression of wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer in Escherichia coli
gene TK1968, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta2 (DE3) pLysS
KPR expressed using a pRSETA vector in Escherichia coli strain BL21(DE3)C41
recombinant expression of C-terminally His-tagged wild-type and mutant enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kataoka, M.; Shimizu, S.; Yamada, H.
Novel enzymic production of D-(-)-pantoyl lactone through the stereospecific reduction of ketopantoic acid
Agric. Biol. Chem.
54
177-182
1990
Agrobacterium sp., Agrobacterium tumefaciens, Stenotrophomonas maltophilia, Pseudomonas putida
-
brenda
Shimizu, S.; Kataoka, M.; Ching-Ming Chung, M.; Yamada, H.
Ketopantoic acid reductase of Pseudomonas maltophilia 845. Purification, characterization, and role in pantothenate biosynthesis
J. Biol. Chem.
263
12077-12084
1988
Saccharomyces cerevisiae, Stenotrophomonas maltophilia, Stenotrophomonas maltophilia 845
brenda
King, H.L.; Wilken, D.R.
Separation and preliminary studies on 2-ketopantoyl lactone and 2-ketopantoic acid reductases of yeast
J. Biol. Chem.
247
4096-4098
1972
Saccharomyces cerevisiae, Saccharomyces cerevisiae NRRL Y-2034
-
brenda
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
Merkamm, M.; Chassagnole, C.; Lindley, N.D.; Guyonvarch, A.
Ketopantoate reductase activity is only encoded by ilvC in Corynebacterium glutamicum
J. Biotechnol.
104
253-260
2003
Corynebacterium glutamicum
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
Miller, C.N.; LoVullo, E.D.; Kijek, T.M.; Fuller, J.R.; Brunton, J.C.; Steele, S.P.; Taft-Benz, S.A.; Richardson, A.R.; Kawula, T.H.
PanG, a new ketopantoate reductase involved in pantothenate synthesis
J. Bacteriol.
195
965-976
2013
Francisella tularensis subsp. novicida
brenda
Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase
Biochem. Biophys. Res. Commun.
439
109-114
2013
Enterococcus faecalis (E3USM3), Enterococcus faecalis IAM10071 (E3USM3), Enterococcus faecalis IAM10071
brenda
Tomita, H.; Imanaka, T.; Atomi, H.
Identification and characterization of an archaeal ketopantoate reductase and its involvement in regulation of coenzyme A biosynthesis
Mol. Microbiol.
90
307-321
2013
Thermococcus kodakarensis (Q5JGC2), Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918 (Q5JGC2)
brenda
Aikawa, Y.; Nishitani, Y.; Tomita, H.; Atomi, H.; Miki, K.
Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP(.)
Acta crystallogr. Sect. F
72
369-375
2016
Thermococcus kodakarensis (Q5JGC2), Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918 (Q5JGC2)
brenda
Sanchez, J.E.; Gross, P.G.; Goetze, R.W.; Walsh, R.M.; Peeples, W.B.; Wood, Z.A.
Evidence of kinetic cooperativity in dimeric ketopantoate reductase from Staphylococcus aureus
Biochemistry
54
3360-3369
2015
Staphylococcus aureus (A0A0J9X283), Staphylococcus aureus
brenda
Aikawa, Y.; Nishitani, Y.; Tomita, H.; Atomi, H.; Miki, K.
Crystal structure of archaeal ketopantoate reductase complexed with coenzyme a and 2-oxopantoate provides structural insights into feedback regulation
Proteins
84
374-382
2016
Thermococcus kodakarensis (Q5JGC2), Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918 (Q5JGC2)
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
Pei, X.; Wang, J.; Zheng, H.; Cheng, P.; Wu, Y.; Wang, A.; Su, W.
Highly efficient asymmetric reduction of ketopantolactone to D-(-)-pantolactone by Escherichia coli cells expressing recombinant conjugated polyketone reductase and glucose dehydrogenase in a fed-batch biphasic reaction system
React. Chem. Eng.
5
531-538
2020
Candida dubliniensis, Candida dubliniensis CD36
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.169)
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