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Information on EC 1.1.1.214 - 2-dehydropantolactone reductase (Si-specific)
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EC Tree
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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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cpr-c2, cpr-c1, conjugated polyketone reductase c2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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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conjugated polyketone reductase
conjugated polyketone reductase C2
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
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nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
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nicotinamide adenine dinucleotide phosphate-dependent ketopantoyl lactone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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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.
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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
keto-omega-methylpantoyl lactone + NADPH
methylpantoyl lactone + NADP+
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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
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
i.e. ketopantoyl lactone
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
i.e. ketopantoyl lactone
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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?
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 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
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
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
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
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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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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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?
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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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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?
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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?
additional information
?
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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
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?
additional information
?
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the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
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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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the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
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?
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
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r
(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 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 strictly stereospecific manner
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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
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
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
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the conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
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evolution
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the conjugated polyketone reductase C2 (CPR-C1) from Candida parapsilosis IFO 0708 belongs to the aldo-keto reductase, AKR, superfamily
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metabolism
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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
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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
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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
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catalytic tetrad in the active site of CPR-C2/NADPH
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additional information
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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
-
H8XA83_CANO9
Candida orthopsilosis (strain 90-125)
307
0
34789
TrEMBL
Chloroplast (Reliability: 2)
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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
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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
D58A
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site-directed mutagenesis, the mutant shows 4.82% of wild-type activity
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H125A
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site-directed mutagenesis, the mutant shows 1.5% of wild-type activity
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K28A
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site-directed mutagenesis, the mutant shows 71.1% of wild-type activity
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K30A
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site-directed mutagenesis, the mutant shows 55.1% of wild-type activity
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R267A
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site-directed mutagenesis, the mutant shows 8.43% 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
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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