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Information on EC 1.1.1.214 - 2-dehydropantolactone reductase (Si-specific) and Organism(s) Candida parapsilosis and UniProt Accession Q76L36
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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.
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The taxonomic range for the selected organisms is: Candida parapsilosis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cpr-c2, cpr-c1, conjugated polyketone reductase c2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
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2-dehydropantoyl-lactone reductase (B-specific)
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2-ketopantoyl lactone reductase
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2-oxopantoyl lactone reductase
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ketopantoyl lactone reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY
37211-75-9
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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
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
i.e. ketopantoyl lactone
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-
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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-
-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
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-
-
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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-
-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
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-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a NADPH-dependent and stereospecific manner.
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r
additional information
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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
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?
additional information
?
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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
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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
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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-
-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
-
-
r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
-
-
-
?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
-
-
-
r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
the enzyme enzyme reduces ketopantoyl lactone to D-pantoyl lactone in a strictly stereospecific manner
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r
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23.6
purified recombinant detagged wild-type enzyme, pH and temperature not specified in the publication
19.3
recombinant isozyme CPR-C1 in cell extract of expressing Escherichia coli cells in absence of IPTG
5.03
recombinant isozyme CPR-C2 in cell extract of expressing Escherichia coli cells in absence of IPTG
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
enzyme is useful for production of chiral alcohols
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q76L36), Candida parapsilosis (Q76L37), Candida parapsilosis, Candida parapsilosis IFO 0708 (Q76L36), Candida parapsilosis IFO 0708 (Q76L37), Candida parapsilosis IFO 0708
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
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
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