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 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 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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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%
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
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
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%
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
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
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
Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate
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
Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding
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
Discovery of a new NADPH-dependent aldo-keto reductase from Candida orthopsilosis catalyzing the stereospecific synthesis of (R)-pantolactone by genome mining
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
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