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Information on EC 1.1.1.358 - 2-dehydropantolactone reductase
for references in articles please use BRENDA:EC1.1.1.358
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.358 2-dehydropantolactone reductase
IUBMB Comments
The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5). This entry covers enzymes whose stereo specificity for NADP+ is not known. cf. EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific) and EC 1.1.1.214, 2-dehydropantolactone reductase (Si-specific).
The enzyme appears in viruses and cellular organisms
- 1.1.1.358
- polyketone
-
chickpea
-
aldo-keto
-
racemic
-
nadph-dependent
-
enantiomeric
- synthesis
-
stereoselective
showSynonyms
cpr-01, corcpr, ketopantoyl-lactone reductase, cducpr, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
-
-
-
-
(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
-
(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+
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+
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+
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+
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+
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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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosphopantothenate biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(R)-pantolactone:NADP+ oxidoreductase
The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5). This entry covers enzymes whose stereo specificity for NADP+ is not known. cf. EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific) and EC 1.1.1.214, 2-dehydropantolactone reductase (Si-specific).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-methylisatin + NADPH + H+
?
-
Substrates: 86% of the activity compared to isatin
Products: -
Products: -
?
5-methylisatin + NADPH + H+
?
-
Substrates: 108% of the activity compared to isatin
Products: -
Products: -
?
camphorquinone + NADPH + H+
?
-
Substrates: 97% of the activity compared to isatin
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 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
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 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
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 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
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: product identification and quantification by gas chromatography. Optimization of the reaction conditions for the synthesis of (R)-(-)-pantolactone
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
NADPH is embedded in the coenzyme binding groove in an extended conformation, and the nicotinamide ring positioned at the bottom of the substrate binding cavity. The adenosine 2'-phosphate group is bound to the side chains of Lys28, Ser263 and Arg267 of CorCPR
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Ni2+ and Ca2+ have almost no influence on the activity of CorCPR
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kintics
-
0.484
2-dehydropantolactone
pH 7.0, 30°C, recombinant wild-type enzyme
0.484
2-dehydropantolactone
pH 7.0, 30°C, recombinant free enzyme
0.886
2-dehydropantolactone
pH 7.0, 30°C, recombinant immobilized enzyme
20.4
2-dehydropantolactone
pH 7.0, 30°C, recombinant mutant H128A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.01
2-dehydropantolactone
pH 7.0, 30°C, recombinant mutant H128A
13.6
2-dehydropantolactone
pH 7.0, 30°C, recombinant immobilized enzyme
59
2-dehydropantolactone
pH 7.0, 30°C, recombinant wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.295
2-dehydropantolactone
pH 7.0, 30°C, recombinant mutant H128A
15.35
2-dehydropantolactone
pH 7.0, 30°C, recombinant immobilized enzyme
121.9
2-dehydropantolactone
pH 7.0, 30°C, recombinant wild-type enzyme
121.9
2-dehydropantolactone
pH 7.0, 30°C, recombinant free enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0014
3,4-Dihydroxy-3-cyclobutene-1,2-dione
-
pH 7.0, 30°C, substrate: isatin
0.0002
cyclohexenediol-1,2,3,4-tetraone
-
pH 7.0, 30°C, substrate: isatin
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
evolution
-
enzyme CorCPR belongs to the AKR3C family of AKR superfamily, it also contains the conserved GXGT/SX motif of the AKR superfamily
evolution
enzyme CduCPR belongs to the aldo-keto reductase superfamily
evolution
-
enzyme CduCPR belongs to the aldo-keto reductase superfamily
-
evolution
-
enzyme CduCPR belongs to the aldo-keto reductase superfamily
-
evolution
-
enzyme CduCPR belongs to the aldo-keto reductase superfamily
-
evolution
-
enzyme CduCPR belongs to the aldo-keto reductase superfamily
-
evolution
-
enzyme CduCPR belongs to the aldo-keto reductase superfamily
-
evolution
-
enzyme CorCPR belongs to the AKR3C family of AKR superfamily, it also contains the conserved GXGT/SX motif of the AKR superfamily
-
additional information
-
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
-
homology modeled structure of CduCPR and molecular docking analysis, overview
additional information
-
homology modeled structure of CduCPR and molecular docking analysis, overview
-
additional information
-
homology modeled structure of CduCPR and molecular docking analysis, overview
-
additional information
-
homology modeled structure of CduCPR and molecular docking analysis, overview
-
additional information
-
homology modeled structure of CduCPR and molecular docking analysis, overview
-
additional information
-
homology modeled structure of CduCPR and molecular docking analysis, overview
-
additional information
-
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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Show AA Sequence and Transmembrane Helices (402 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34491
x * 34491, isoform CPR-C1, calculated from amino acid sequence
34650
x * 34650, isoform CPR-C2, calculated from amino acid sequence
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 37000, about, recombinant His6-tagged enzyme, sequence calculation and SDS-PAGE
?
-
x * 37000, about, recombinant His6-tagged enzyme, sequence calculation and SDS-PAGE
-
?
x * 34650, isoform CPR-C2, calculated from amino acid sequence
?
x * 34491, isoform CPR-C1, calculated from amino acid sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with NADPH, sitting drop vapor diffusion method, using 0.1 M TrisHCl (pH 8.1) and 23% (w/v) polyethylene glycol 3350, at 20°C
sitting drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5), 25% (w/v) PEG3350, and 0.2 M NaCl
sitting drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.1 and 23% (w/v) PEG 3350
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H128A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
T30A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
T30A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
T30A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
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T30A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
T30A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
T30A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
additional information
additional information
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview
additional information
-
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview
-
additional information
-
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview
-
additional information
-
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview
-
additional information
-
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview
-
additional information
-
an effective biocatalytic cascade was developed by encapsulating a conjugated polyketone reductase (CPR), glucose dehydrogenase (GDH) and the coenzyme NADP+ in organic-inorganic hybrid nanoflowers (hNFs) for the asymmetric reduction of oxopantolactone (KPL) to synthesize (R)-(-)-pantolactone ((R)-PL). When CduCPR and TgGDH are confined in the sodium alginate (SA)-coated hNFs [CduCPR/TgGDH-Ca3(PO4)2], both of them have excellent reusability and high stability. The SA-coated hNF reactor successfully catalyzes the asymmetric synthesis of (R)-PL, which exhibits satisfactory stereoselectivity and promotes reusability in repeated batches. The SA coating functioned to competently immobilize the coenzyme NADP+ on the CduCPR/TgGDH-Ca3(PO4)2 hNFs, which maintains the maximum bioactivity to synthesize (R)-PL without exogenous coenzyme addition. Method development, optimization, and evaluation, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
purified recombinant His-tagged enzyme, pH 7.0, 7 h, about 90% activity remaining
40
40 - 50
-
purified recombinant His6-tagged enzyme, pH 7.0, half-lives of the enzyme at 40, 45 and 50°C are 6.3 h, 3.7 h and 52 min, respectively
50
purified recombinant His-tagged enzyme, pH 7.0, 7 h, about 10% activity remaining
40
purified recombinant His-tagged enzyme, pH 7.0, 7 h, about 50% activity remaining
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni Sepharose column chromatography and Superdex 75 gel filtration
Ni Sepharose column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CPR-C2, functional overexpression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene CPR-C2, functional overexpression of N-terminally His6-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His6-tagged enzyme mutants in Escherichia coli
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
the enzyme has a potential application in the asymmetric synthesis of optically active (R)-pantothenate, synthetic method of (R)-pantothenate production through the stereoselective reduction of oxopantoyl lactone (KPL) by aldo-keto reductase (AKR). (R)-Pantolactone (PL) is a key chiral building block for the synthesis of calcium (R)-pantothenate (vitamin B5), (R)-panthenol, and (R)-pantetheine, which are used as food and feed additives, as well as ingredients in pharmaceutical and cosmetic compositions
synthesis
the recombinant CduCPR from Candida dubliniensis exhibits potential application in the asymmetric synthesis of (R)-pantolactone
synthesis
-
the recombinant CduCPR from Candida dubliniensis exhibits potential application in the asymmetric synthesis of (R)-pantolactone
-
synthesis
-
the recombinant CduCPR from Candida dubliniensis exhibits potential application in the asymmetric synthesis of (R)-pantolactone
-
synthesis
-
the recombinant CduCPR from Candida dubliniensis exhibits potential application in the asymmetric synthesis of (R)-pantolactone
-
synthesis
-
the recombinant CduCPR from Candida dubliniensis exhibits potential application in the asymmetric synthesis of (R)-pantolactone
-
synthesis
-
the recombinant CduCPR from Candida dubliniensis exhibits potential application in the asymmetric synthesis of (R)-pantolactone
-
synthesis
-
the enzyme has a potential application in the asymmetric synthesis of optically active (R)-pantothenate, synthetic method of (R)-pantothenate production through the stereoselective reduction of oxopantoyl lactone (KPL) by aldo-keto reductase (AKR). (R)-Pantolactone (PL) is a key chiral building block for the synthesis of calcium (R)-pantothenate (vitamin B5), (R)-panthenol, and (R)-pantetheine, which are used as food and feed additives, as well as ingredients in pharmaceutical and cosmetic compositions
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hata, H.; Shimizu, S.; Hattori, S.; Yamada, H.
Ketopantoyl-lactone reductase from Candida parapsilosis: purification and characterization as a conjugated polyketone reductase
Biochim. Biophys. Acta
990
175-181
1989
Candida parapsilosis, Candida parapsilosis IFO 0708
brenda
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
Appl. Microbiol. Biotechnol.
64
359-366
2004
Candida parapsilosis (Q76L37), Candida parapsilosis (Q76L36), Candida parapsilosis IFO 0708 (Q76L37), Candida parapsilosis IFO 0708 (Q76L36)
brenda
Yamamura, A.; Maruoka, S.; Ohtsuka, J.; Miyakawa, T.; Nagata, K.; Kataoka, M.; Kitamura, N.; Shimizu, S.; Tanokura, M.
Expression, purification, crystallization and preliminary X-ray analysis of conjugated polyketone reductase C2 (CPR-C2) from Candida parapsilosis IFO 0708
Acta Crystallogr. Sect. F
65
1145-1148
2009
Candida parapsilosis (Q76L36), Candida parapsilosis IFO 0708 (Q76L36)
brenda
Qin, H.M.; Yamamura, A.; Miyakawa, T.; Kataoka, M.; Nagai, T.; Kitamura, N.; Urano, N.; Maruoka, S.; Ohtsuka, J.; Nagata, K.; Shimizu, S.; Tanokura, M.
Structure of conjugated polyketone reductase from Candida parapsilosis IFO 0708 reveals conformational changes for substrate recognition upon NADPH binding
Appl. Microbiol. Biotechnol.
98
243-249
2013
Candida parapsilosis (Q76L36), Candida parapsilosis IFO 0708 (Q76L36)
brenda
Qin, H.M.; Yamamura, A.; Miyakawa, T.; Kataoka, M.; Maruoka, S.; Ohtsuka, J.; Nagata, K.; Shimizu, S.; Tanokura, M.
Crystal structure of conjugated polyketone reductase (CPR-C1) from Candida parapsilosis IFO 0708 complexed with NADPH
Proteins
81
2059-2063
2013
Candida parapsilosis (Q76L36), Candida parapsilosis IFO 0708 (Q76L36)
brenda
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
Enzyme Microb. Technol.
126
77-85
2019
Candida dubliniensis (B9WJQ5), Candida dubliniensis, Candida dubliniensis ATCC MYA-646 (B9WJQ5), Candida dubliniensis CBS 7987 (B9WJQ5), Candida dubliniensis CD36 (B9WJQ5), Candida dubliniensis CD36, Candida dubliniensis NCPF 3949 (B9WJQ5), Candida dubliniensis NRRL Y-17841 (B9WJQ5)
brenda
Wang, J.; Cheng, P.; Wu, Y.; Wang, A.; Liu, F.; Pei, X.
Discovery of a new NADPH-dependent aldo-keto reductase from Candida orthopsilosis catalyzing the stereospecific synthesis of (R)-pantolactone by genome mining
J. Biotechnol.
291
26-34
2019
Candida orthopsilosis, Candida orthopsilosis Co 90-125
brenda
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
React. Chem. Eng.
5
1973-1980
2020
Candida dubliniensis (B9WJQ5), Candida dubliniensis ATCC MYA-646 (B9WJQ5), Candida dubliniensis CBS 7987 (B9WJQ5), Candida dubliniensis CD36 (B9WJQ5), Candida dubliniensis NCPF 3949 (B9WJQ5), Candida dubliniensis NRRL Y-17841 (B9WJQ5)
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.358)
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