Information on EC 1.1.1.214 - 2-dehydropantolactone reductase (Si-specific)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.214
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RECOMMENDED NAME
GeneOntology No.
2-dehydropantolactone reductase (Si-specific)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37211-75-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
show the reaction diagram
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
show the reaction diagram
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
acenaphthenequinone
?
show the reaction diagram
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?
bornanedione + NADPH
?
show the reaction diagram
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?
isatin + NADPH
?
show the reaction diagram
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?
keto-omega-methylpantoyl lactone + NADPH
methylpantoyl lactone + NADP+
show the reaction diagram
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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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?
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH
show the reaction diagram
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
show the reaction diagram
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
ketopantoyl lactone + NADPH
pantoyl lactone + NADP+
show the reaction diagram
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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no activity observed with NADH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-pantolactone
substrate inhibition of the recombinant isozyme expressed in Escherichia coli at a concentration above 10 mg/ml
2-keto-4-hydroxybutyrolactone
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strong and uncompetitive inhibitor
substituted 2,5-dioxopyrrolidines
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strong and uncompetitive inhibitors
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.03
recombinant isozyme CPR-C2 in cell extract of expressing Escherichia coli cells in absence of IPTG
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
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000 - 36000
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36000
x * 36000, recombinant isozyme CPR-C2, SDS-PAGE
38000
x * 38000, recombinant isozyme CPR-C1, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 33000-36000
additional information
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 Tris–HCl, 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
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
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
K88A
site-directed mutagenesis, inactive mutant
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis