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conjugated polyketone reductase
conjugated polyketone reductase C2
ketopantoyl-lactone reductase
NADPH-dependent conjugated polyketone reductase
NADPH-dependent ketopantoyl lactone reductase
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CduCPR
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase
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conjugated polyketone reductase C2
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conjugated polyketone reductase C2
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CorCPR
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CPR
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CPR-01
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CPR-C1
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CPR-C2
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ketopantoyl-lactone reductase
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ketopantoyl-lactone reductase
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NADPH-dependent conjugated polyketone reductase
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NADPH-dependent conjugated polyketone reductase
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NADPH-dependent conjugated polyketone reductase
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NADPH-dependent conjugated polyketone reductase
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NADPH-dependent conjugated polyketone reductase
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NADPH-dependent conjugated polyketone reductase
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
catalytic mechanism of (R)-pantolactone synthesis, overview. The conserved catalytic triad is formed by residues Thr30, Tyr66 and His128. Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient 2-dehydropantolactone (KPL). The phenolic hydroxyl group of Tyr66 forms the hydrogen bond with the C5 carbonyl oxygen of 2-dehydropantolactone. The HR of NADPH could just attack the si-face of the carbonyl group, which results in the formation of (R)-pantolactone. The alpha-amino group and the hydroxyl group of Thr30 form hydrogen bonds with the C4 carbonyl oxygen of KPL, and the epsilon-amino group of Lys33 formes the hydrogen bond with the O2 of KPL. In addition, the hydrophobic interaction of His128, Val165 and Phe302 with two methyl groups of KPL might facilitate the substrate binding
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
enzyme CorCPR has a catalytic tetrad D-Y-K-H, and the detailed catalytic mechanism is clarified by molecular docking, overview
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
catalytic mechanism of (R)-pantolactone synthesis, overview. The conserved catalytic triad is formed by residues Thr30, Tyr66 and His128. Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient 2-dehydropantolactone (KPL). The phenolic hydroxyl group of Tyr66 forms the hydrogen bond with the C5 carbonyl oxygen of 2-dehydropantolactone. The HR of NADPH could just attack the si-face of the carbonyl group, which results in the formation of (R)-pantolactone. The alpha-amino group and the hydroxyl group of Thr30 form hydrogen bonds with the C4 carbonyl oxygen of KPL, and the epsilon-amino group of Lys33 formes the hydrogen bond with the O2 of KPL. In addition, the hydrophobic interaction of His128, Val165 and Phe302 with two methyl groups of KPL might facilitate the substrate binding
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
catalytic mechanism of (R)-pantolactone synthesis, overview. The conserved catalytic triad is formed by residues Thr30, Tyr66 and His128. Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient 2-dehydropantolactone (KPL). The phenolic hydroxyl group of Tyr66 forms the hydrogen bond with the C5 carbonyl oxygen of 2-dehydropantolactone. The HR of NADPH could just attack the si-face of the carbonyl group, which results in the formation of (R)-pantolactone. The alpha-amino group and the hydroxyl group of Thr30 form hydrogen bonds with the C4 carbonyl oxygen of KPL, and the epsilon-amino group of Lys33 formes the hydrogen bond with the O2 of KPL. In addition, the hydrophobic interaction of His128, Val165 and Phe302 with two methyl groups of KPL might facilitate the substrate binding
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
enzyme CorCPR has a catalytic tetrad D-Y-K-H, and the detailed catalytic mechanism is clarified by molecular docking, overview
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
catalytic mechanism of (R)-pantolactone synthesis, overview. The conserved catalytic triad is formed by residues Thr30, Tyr66 and His128. Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient 2-dehydropantolactone (KPL). The phenolic hydroxyl group of Tyr66 forms the hydrogen bond with the C5 carbonyl oxygen of 2-dehydropantolactone. The HR of NADPH could just attack the si-face of the carbonyl group, which results in the formation of (R)-pantolactone. The alpha-amino group and the hydroxyl group of Thr30 form hydrogen bonds with the C4 carbonyl oxygen of KPL, and the epsilon-amino group of Lys33 formes the hydrogen bond with the O2 of KPL. In addition, the hydrophobic interaction of His128, Val165 and Phe302 with two methyl groups of KPL might facilitate the substrate binding
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
catalytic mechanism of (R)-pantolactone synthesis, overview. The conserved catalytic triad is formed by residues Thr30, Tyr66 and His128. Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient 2-dehydropantolactone (KPL). The phenolic hydroxyl group of Tyr66 forms the hydrogen bond with the C5 carbonyl oxygen of 2-dehydropantolactone. The HR of NADPH could just attack the si-face of the carbonyl group, which results in the formation of (R)-pantolactone. The alpha-amino group and the hydroxyl group of Thr30 form hydrogen bonds with the C4 carbonyl oxygen of KPL, and the epsilon-amino group of Lys33 formes the hydrogen bond with the O2 of KPL. In addition, the hydrophobic interaction of His128, Val165 and Phe302 with two methyl groups of KPL might facilitate the substrate binding
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
catalytic mechanism of (R)-pantolactone synthesis, overview. The conserved catalytic triad is formed by residues Thr30, Tyr66 and His128. Tyr66 functions as a proton donor following hydrogen transfer from NADPH. Thr30 and His128 are critical residues to bind and orient 2-dehydropantolactone (KPL). The phenolic hydroxyl group of Tyr66 forms the hydrogen bond with the C5 carbonyl oxygen of 2-dehydropantolactone. The HR of NADPH could just attack the si-face of the carbonyl group, which results in the formation of (R)-pantolactone. The alpha-amino group and the hydroxyl group of Thr30 form hydrogen bonds with the C4 carbonyl oxygen of KPL, and the epsilon-amino group of Lys33 formes the hydrogen bond with the O2 of KPL. In addition, the hydrophobic interaction of His128, Val165 and Phe302 with two methyl groups of KPL might facilitate the substrate binding
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1-methylisatin + NADPH + H+
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86% of the activity compared to isatin
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
5-methylisatin + NADPH + H+
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108% of the activity compared to isatin
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camphorquinone + NADPH + H+
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97% of the activity compared to isatin
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isatin + NADPH + H+
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additional information
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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+
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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+
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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recombinant CorCPR exhibited a high catalytic activity for the synthesis of (R)-pantolactone ((R)-PL) from 2-dehydropantolactone (KPL). The activity assay is performed using purified CorCPR and crude recombinant GDH in a single batch reaction. GDH is used to complete the enzyme-coupled NADPH regeneration system. CPR-01 form Candida orthopsilosis Co 90-125 exhibits excellent enantioselectivity (enantiomeric excess of over 99%). CorCPR exhibits the highest activity and stereoselectivity toward KPL
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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recombinant CorCPR exhibited a high catalytic activity for the synthesis of (R)-pantolactone ((R)-PL) from 2-dehydropantolactone (KPL). The activity assay is performed using purified CorCPR and crude recombinant GDH in a single batch reaction. GDH is used to complete the enzyme-coupled NADPH regeneration system. CPR-01 form Candida orthopsilosis Co 90-125 exhibits excellent enantioselectivity (enantiomeric excess of over 99%). CorCPR exhibits the highest activity and stereoselectivity toward KPL
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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+
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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69% of the activity compared to isatin. The stereospecificity for NADPH is not known. Activity with NADH is 2% compared to the activity with NADPH
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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+
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
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additional information
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enzyme CduCPR shows high catalytic activity and stereoselectivity using 2-dehydropantolactone (KPL) as the substrate. In a continuous feeding reaction, 200 mM ketopantolactone is reduced to (R)-pantolactone with 98% conversion and 99% enantiomeric excess within 2.0 h by the purified recombinant enzyme
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additional information
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product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
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additional information
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the aldo-keto reductase (AKR) can catalyze ketopantoyl lactone to optically active (R)-pantolactone. A putative catalytic mechanism is proposed that Tyr63 acts as a general acid. No activity of recombinant CorCPR with typical AKR substrates such as p-nitrobenzaldehyde. Other alpha-oxoesters are not the optimal substrates of CorCPR due to the relatively low activities and low stereoselectivities
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additional information
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the aldo-keto reductase (AKR) can catalyze ketopantoyl lactone to optically active (R)-pantolactone. A putative catalytic mechanism is proposed that Tyr63 acts as a general acid. No activity of recombinant CorCPR with typical AKR substrates such as p-nitrobenzaldehyde. Other alpha-oxoesters are not the optimal substrates of CorCPR due to the relatively low activities and low stereoselectivities
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2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
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+
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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+
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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+
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ir
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+
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ir
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+
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0.19
2-dehydropantolactone
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pH 7.0, 30°C, substrate: isatin
0.0014
3,4-Dihydroxy-3-cyclobutene-1,2-dione
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pH 7.0, 30°C, substrate: isatin
0.0002
cyclohexenediol-1,2,3,4-tetraone
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pH 7.0, 30°C, substrate: isatin
3.14
parabanic acid
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pH 7.0, 30°C, substrate: isatin
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evolution
enzyme CduCPR belongs to the aldo-keto reductase superfamily
evolution
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enzyme CorCPR belongs to the AKR3C family of AKR superfamily, it also contains the conserved GXGT/SX motif of the AKR superfamily
evolution
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enzyme CduCPR belongs to the aldo-keto reductase superfamily
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evolution
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enzyme CduCPR belongs to the aldo-keto reductase superfamily
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evolution
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enzyme CorCPR belongs to the AKR3C family of AKR superfamily, it also contains the conserved GXGT/SX motif of the AKR superfamily
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evolution
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enzyme CduCPR belongs to the aldo-keto reductase superfamily
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evolution
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enzyme CduCPR belongs to the aldo-keto reductase superfamily
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evolution
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enzyme CduCPR belongs to the aldo-keto reductase superfamily
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additional information
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docking analysis and structure homology modeling of CorCPR, the crystal structure of CPR-C2 from Candida parapsilosis strain IFO 0708 (PDB ID 3VXG, resolution 1.7 A) is used as the model structure, overview. KPL is docked into the substrate binding pocket. The model predicts that the C3 carbonyl oxygen of KPL forms hydrogen bond with the side chains of Tyr63, and the alpha-amino group of Thr27 also forms a hydrogen bond with C2 carbonyl oxygen. The catalytic tetrads of CorCPR are Asp58, Tyr63, Lys88 and His125. Tyr63 acts as a general acid, and His125 facilitates proton donation, the phenolic hydroxy group of Tyr63 provide general acid catalytic assistance to carbonyl group of KPL, and residues Asp 58 and Tys88 are responsible for the hydrogen transfer. The stereospecificity of CorCPR is respected to the pro-R hydrogen at C4 of the nicotinamide ring and the pseudo re-side attack of the hydride on the carbonyl group. In addition, the formation of hydrogen bond between Thr27 and the C2 carbonyl oxygen of KPL plays an important role in substrate recognition
additional information
homology modeled structure of CduCPR and molecular docking analysis, overview
additional information
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homology modeled structure of CduCPR and molecular docking analysis, overview
additional information
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homology modeled structure of CduCPR and molecular docking analysis, overview
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additional information
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homology modeled structure of CduCPR and molecular docking analysis, overview
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additional information
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docking analysis and structure homology modeling of CorCPR, the crystal structure of CPR-C2 from Candida parapsilosis strain IFO 0708 (PDB ID 3VXG, resolution 1.7 A) is used as the model structure, overview. KPL is docked into the substrate binding pocket. The model predicts that the C3 carbonyl oxygen of KPL forms hydrogen bond with the side chains of Tyr63, and the alpha-amino group of Thr27 also forms a hydrogen bond with C2 carbonyl oxygen. The catalytic tetrads of CorCPR are Asp58, Tyr63, Lys88 and His125. Tyr63 acts as a general acid, and His125 facilitates proton donation, the phenolic hydroxy group of Tyr63 provide general acid catalytic assistance to carbonyl group of KPL, and residues Asp 58 and Tys88 are responsible for the hydrogen transfer. The stereospecificity of CorCPR is respected to the pro-R hydrogen at C4 of the nicotinamide ring and the pseudo re-side attack of the hydride on the carbonyl group. In addition, the formation of hydrogen bond between Thr27 and the C2 carbonyl oxygen of KPL plays an important role in substrate recognition
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additional information
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homology modeled structure of CduCPR and molecular docking analysis, overview
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additional information
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homology modeled structure of CduCPR and molecular docking analysis, overview
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additional information
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homology modeled structure of CduCPR and molecular docking analysis, overview
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1.1.1.358 2-dehydropantolactone reductase
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