1.1.1.358: 2-dehydropantolactone reductase
This is an abbreviated version!
For detailed information about 2-dehydropantolactone reductase, go to the full flat file.
Word Map on EC 1.1.1.358
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1.1.1.358
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polyketone
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chickpea
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aldo-keto
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racemic
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nadph-dependent
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enantiomeric
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synthesis
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stereoselective
- 1.1.1.358
- polyketone
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chickpea
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aldo-keto
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racemic
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nadph-dependent
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enantiomeric
- synthesis
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stereoselective
Reaction
Synonyms
CduCPR, conjugated polyketone reductase, conjugated polyketone reductase C2, CorCPR, CPR, CPR-01, CPR-C1, CPR-C2, ketopantoyl-lactone reductase, NADPH-dependent conjugated polyketone reductase, NADPH-dependent ketopantoyl lactone reductase
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Substrates Products
Substrates Products on EC 1.1.1.358 - 2-dehydropantolactone reductase
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REACTION DIAGRAM
1-methylisatin + NADPH + H+
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86% of the activity compared to isatin
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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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(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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ir
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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ir
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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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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