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Information on EC 1.1.1.214 - 2-dehydropantolactone reductase (Si-specific)
for references in articles please use BRENDA:EC1.1.1.214
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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
1.1.1.214 2-dehydropantolactone reductase (Si-specific)
IUBMB Comments
The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific)], which is specific for the Re-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
cpr-c2, cpr-c1, conjugated polyketone reductase c2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-dehydropantoyl-lactone reductase (B-specific)
-
-
-
-
2-ketopantoyl lactone reductase
-
-
-
-
2-oxopantoyl lactone reductase
-
-
-
-
conjugated polyketone reductase
CORT_0G03830
CPR
CPR-C1
CPR-C2
ketopantoyl lactone reductase
NADPH-dependent conjugated polyketone reductase
NADPH-dependent ketopantoyl lactone reductase
nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
ketopantoyl lactone reductase
-
-
-
-
nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
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nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
-
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosphopantothenate biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(R)-pantolactone:NADP+ oxidoreductase (Si-specific)
The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific)], which is specific for the Re-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
37211-75-9
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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
keto-omega-methylpantoyl lactone + NADPH
methylpantoyl lactone + NADP+
-
Substrates: the only compound other than ketopantoyl lactone which is a substrate, 73% relative activity to ketopantoyl lactone with form A enzyme, 56% relative activity to ketopantoyl lactone with form B enzyme
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
Substrates: -
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
Substrates: i.e. ketopantoyl lactone
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
Substrates: -
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
Substrates: i.e. ketopantoyl lactone
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
Products: -
Products: -
r
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
-
Substrates: -
Products: the enzyme is involved in pantothenate biosynthesis, pantoyl lactone, the putative product of the reaction, together with beta-alanine and ATP are the substrate of pantothenate synthase
Products: the enzyme is involved in pantothenate biosynthesis, pantoyl lactone, the putative product of the reaction, together with beta-alanine and ATP are the substrate of pantothenate synthase
?
additional information
?
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Substrates: structural basis of the substrate specificity, overview. Enzyme CPR-C2 adopts a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induces conformational changes in which Thr27 and Lys28 move 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds, substrate binding modeling
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
Products: -
Products: -
?
additional information
?
-
Substrates: structural basis of the substrate specificity, overview. Enzyme CPR-C2 adopts a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induces conformational changes in which Thr27 and Lys28 move 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds, substrate binding modeling
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural basis of the substrate specificity, overview. Enzyme CPR-C2 adopts a triose-phosphate isomerase barrel fold at the core of the structure. Binding with the cofactor NADPH induces conformational changes in which Thr27 and Lys28 move 15 and 5.0 A, respectively, in the close vicinity of the adenosine 2'-phosphate group of NADPH to form hydrogen bonds, substrate binding modeling
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not reduce typical AKR substrates such as 4-nitrobenzaldehyde and pyridine-3-aldehyde, but does reduce alpha-diketones such as ketopantoyl lactone to D-pantoyl lactone in a stereospecific manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: both forms of the enzyme are B-specific, the enzyme exhibits opposite stereospecificity from that observed with the Saccharomyces cerevisiae enzyme, which is A-specific, less than 5% relative activity to ketopantoyl lactone with the following 2-keto-gamma-lactones: 2-keto-4-hydroxy-3-methylbutyric acid-gamma-lactone, 2-keto-4-hydroxybutyric acid-gamma-lactone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
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
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
-
Substrates: -
Products: the enzyme is involved in pantothenate biosynthesis, pantoyl lactone, the putative product of the reaction, together with beta-alanine and ATP are the substrate of pantothenate synthase
Products: the enzyme is involved in pantothenate biosynthesis, pantoyl lactone, the putative product of the reaction, together with beta-alanine and ATP are the substrate of pantothenate synthase
?
additional information
?
-
-
Substrates: the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
Substrates: -
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
Substrates: -
Products: -
Products: -
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
Substrates: -
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
CPR-C1 has a conserved GXGTX motif, but a binding mode for recognizing the adenosine 2'-phosphate group of NADPH, binding structure, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-pantolactone
substrate inhibition of the recombinant isozyme expressed in Escherichia coli at a concentration above 10 mg/ml
Mg2+
1 mM, 67.6% residual activity; 1 mM, 80.2% residual activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19.3
recombinant isozyme CPR-C1 in cell extract of expressing Escherichia coli cells in absence of IPTG
23.6
purified recombinant detagged wild-type enzyme, pH and temperature not specified in the publication
5.03
recombinant isozyme CPR-C2 in cell extract of expressing Escherichia coli cells in absence of IPTG
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme CPR-C1; 2 isozymes CPR-C1 and CPR-C2
SwissProt
brenda
isozyme CPR-C2; 2 isozymes CPR-C1 and CPR-C2
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
metabolism
additional information
evolution
the conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
evolution
the conjugated polyketone reductase C2 (CPR-C1) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
evolution
-
the conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
-
evolution
-
the conjugated polyketone reductase C2 (CPR-C1) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
-
metabolism
-
residue Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient substrate 2-dehydropantolactone
metabolism
-
residue Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient substrate 2-dehydropantolactone
-
additional information
catalytic tetrad in the active site of CPR-C2/NADPH
additional information
CPR-C1 adopted a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH. Homology structure modeling, overview
additional information
-
catalytic tetrad in the active site of CPR-C2/NADPH
-
additional information
-
CPR-C1 adopted a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH. Homology structure modeling, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). B9WJQ5_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
309
0
35183
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
CPR-C1 has 12 alpha-helices, 10 beta-strands, and five 310-helices, and adopts a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH
additional information
-
CPR-C1 has 12 alpha-helices, 10 beta-strands, and five 310-helices, and adopts a triose-phosphate isomerase (TIM) barrel fold at the core of the structure in which Thr25 and Lys26 of the GXGTX motif bind uniquely to the adenosine 2-phosphate group of NADPH
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and docking analysis. Structure reveals a triosephosphate isomerase barrel fold comprised of eight beta-strands and eight alpha-helices
purified enzyme in apoform and in complex with NADPH, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution consisting of 0.1 M Tris-HCl, pH 8.1, and 23% w/v PEG 3350 at 20°C, for the enzyme-NADPH complexed crystals, the protein in 20 mM Tris-HCl, pH 8.0, and 5 mM MADPH, is mixed with 0.1 M TrisHCl, pH 7.4, and 256% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.70 A and 1.80 A resolution, respectively, molecular replacement method
purified enzyme in complex with NADPH, sitting drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 5 mM NADPH, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 25% w/v PEG 3350, and 0.2 M NaCl, 20°C, 2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement and modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D58A
site-directed mutagenesis, the mutant shows 4.82% of wild-type activity
F299A
site-directed mutagenesis, the mutant shows 19.1% of wild-type activity
F300A
site-directed mutagenesis, the mutant shows 17.8% of wild-type activity
H125A
site-directed mutagenesis, the mutant shows 1.5% of wild-type activity
K264A
site-directed mutagenesis, the mutant shows 65.7% of wild-type activity
K28A
site-directed mutagenesis, the mutant shows 71.1% of wild-type activity
K30A
site-directed mutagenesis, the mutant shows 55.1% of wild-type activity
R267A
site-directed mutagenesis, the mutant shows 8.43% of wild-type activity
T27A
site-directed mutagenesis, the mutant shows 5.75% of wild-type activity
Y63A
site-directed mutagenesis, the mutant shows 0.17% of wild-type activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
form A and form B of the enzyme obtained separated by rupture, centrifugation and column chromatography on DEAE-cellulose and hydroxylapatite
-
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography, and tag cleavage by thrombin, followed by anion exchange chromatography, gel filtration, and dialysis
using affinity chromatography on Red-Agarose and several subsequent ion exchange steps
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene cpr-c2, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
isozyme CPR-C2, DNA and amino acid sequence determination and analysis, overexpression of the isozyme in Escherichia coli strain BL21(DE3), addition of IPTG highly decreases the expression rate of the isozyme
isozymes CPR-C1, DNA and amino acid sequence determination and analysis, overexpression of the isozyme in Escherichia coli strain BL21(DE3), addition of IPTG highly decreases the expression rate of the isozyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
enzyme is useful for production of chiral alcohols
synthesis
-
in a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h
synthesis
whole-cell biotransformation process to produce D-pantolactone in a biphasic reaction system. Recombinant CPR and glucose dehydrogenase are co-expressed in Escherichia coli to simultaneously achieve the synthesis of D-PL and the regeneration of NADPH. Presence of 15% dichloromethane significantly inhibits the hydrolysis of ketopantolactone. In a fed-batch system, the D-pantolactone concentration reaches 0.77 mol per l in the reaction mixture at 7 h, and its enantiomeric excess is 99%
synthesis
use of polyketone reductase (CPR), glucose dehydrogenase (GDH) and coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of ketopantolactone to synthesize (R)-(-)-pantolactone. The sodium alginate-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-pantolactone, with satisfactory stereoselectivity and reusability in repeated batches
synthesis
-
whole-cell biotransformation process to produce D-pantolactone in a biphasic reaction system. Recombinant CPR and glucose dehydrogenase are co-expressed in Escherichia coli to simultaneously achieve the synthesis of D-PL and the regeneration of NADPH. Presence of 15% dichloromethane significantly inhibits the hydrolysis of ketopantolactone. In a fed-batch system, the D-pantolactone concentration reaches 0.77 mol per l in the reaction mixture at 7 h, and its enantiomeric excess is 99%
-
synthesis
-
use of polyketone reductase (CPR), glucose dehydrogenase (GDH) and coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of ketopantolactone to synthesize (R)-(-)-pantolactone. The sodium alginate-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-pantolactone, with satisfactory stereoselectivity and reusability in repeated batches
-
synthesis
-
in a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h
-
synthesis
-
use of polyketone reductase (CPR), glucose dehydrogenase (GDH) and coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of ketopantolactone to synthesize (R)-(-)-pantolactone. The sodium alginate-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-pantolactone, with satisfactory stereoselectivity and reusability in repeated batches
-
synthesis
-
use of polyketone reductase (CPR), glucose dehydrogenase (GDH) and coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of ketopantolactone to synthesize (R)-(-)-pantolactone. The sodium alginate-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-pantolactone, with satisfactory stereoselectivity and reusability in repeated batches
-
synthesis
-
use of polyketone reductase (CPR), glucose dehydrogenase (GDH) and coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of ketopantolactone to synthesize (R)-(-)-pantolactone. The sodium alginate-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-pantolactone, with satisfactory stereoselectivity and reusability in repeated batches
-
synthesis
-
use of polyketone reductase (CPR), glucose dehydrogenase (GDH) and coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of ketopantolactone to synthesize (R)-(-)-pantolactone. The sodium alginate-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-pantolactone, with satisfactory stereoselectivity and reusability in repeated batches
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Escherichia coli
brenda
Julliard, J.H.
Purification and characterization of oxopantoyl lactone reductase from higher plants: role in pantothenate synthesis
Bot. Acta
107
191-200
1994
Spinacia oleracea
-
brenda
Kataoka, M.; Delacruz-Hidalgo, A.R.G.; Akond, M.A.; Sakuradani, E.; Kita, K.; Shimizu, S.
Gene cloning and overexpression of two conjugated polyketone reductases, novel aldo-keto reductase family enzymes, of Candida parapsilosis. Investigation of hydroxamic acids as laccase-mediators for pulp bleaching
Appl. Microbiol. Biotechnol.
64
359-366
2004
Candida parapsilosis (Q76L37), Candida parapsilosis (Q76L36), Candida parapsilosis, Candida parapsilosis IFO 0708 (Q76L37), Candida parapsilosis IFO 0708 (Q76L36), Candida parapsilosis IFO 0708
brenda
Qin, H.M.; Yamamura, A.; Miyakawa, T.; Kataoka, M.; Nagai, T.; Kitamura, N.; Urano, N.; Maruoka, S.; Ohtsuka, J.; Nagata, K.; Shimizu, S.; Tanokura, M.
Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding
Appl. Microbiol. Biotechnol.
98
243-249
2013
Candida parapsilosis (Q76L36), Candida parapsilosis IFO 0708 (Q76L36), Candida parapsilosis IFO 0708
brenda
Qin, H.M.; Yamamura, A.; Miyakawa, T.; Kataoka, M.; Maruoka, S.; Ohtsuka, J.; Nagata, K.; Shimizu, S.; Tanokura, M.
Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH
Proteins
81
2059-2063
2013
Candida parapsilosis (Q76L37), Candida parapsilosis IFO 0708 (Q76L37), Candida parapsilosis IFO 0708
brenda
Cheng, P.; Wang, J.; Wu, Y.; Jiang, X.; Pei, X.; Su, W.
Recombinant expression and molecular insights into the catalytic mechanism of an NADPH-dependent conjugated polyketone reductase for the asymmetric synthesis of (R)-pantolactone
Enzyme Microb. Technol.
126
77-85
2019
Candida dubliniensis, Candida dubliniensis CD36
brenda
Wang, J.; Cheng, P.; Wu, Y.; Wang, A.; Liu, F.; Pei, X.
Discovery of a new NADPH-dependent aldo-keto reductase from Candida orthopsilosis catalyzing the stereospecific synthesis of (R)-pantolactone by genome mining
J. Biotechnol.
291
26-34
2019
Candida orthopsilosis (H8XA83), Candida orthopsilosis 90-125 (H8XA83)
brenda
Cheng, P.; Tang, M.; Chen, Z.; Liu, W.; Jiang, X.; Pei, X.; Su, W.
Dual-enzyme and NADPH co-embedded organic-inorganic hybrid nanoflowers prepared using biomimetic mineralization for the asymmetric synthesis of ( R)-(-)-pantolactone
React. Chem. Eng.
5
1973-1980
2020
Candida dubliniensis (B9WJQ5), Candida dubliniensis CD36 (B9WJQ5)
-
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 (B9WJQ5), Candida dubliniensis CD36 (B9WJQ5)
-
brenda
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