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Information on EC 1.1.1.168 - 2-dehydropantolactone reductase (Re-specific)
for references in articles please use BRENDA:EC1.1.1.168
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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
1.1.1.168 2-dehydropantolactone reductase (Re-specific)
IUBMB Comments
The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
The enzyme appears in viruses and cellular organisms
showSynonyms
nadph-dependent aldo-keto reductase, ketopantoyl lactone reductase, nadph-dependent conjugated polyketone reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-pantoyl-lactone:NADP+ oxidoreductase (A-specific)
-
-
-
-
2-dehydropantoyl-lactone reductase
-
-
-
-
2-dehydropantoyl-lactone reductase (A-specific)
-
-
-
-
2-ketopantoyl lactone reductase
-
-
-
-
AKR
CPR
ketopantoyl lactone reductase
-
-
-
-
NADPH-dependent aldo-keto reductase
NADPH-dependent conjugated polyketone reductase
reductase, 2-oxopantoyl lactone
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosphopantothenate biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(R)-pantolactone:NADP+ oxidoreductase (Re-specific)
The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
37211-75-9
-
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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
dihydro-4,4-diethyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
dihydro-4-methyl-4-propyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
dihydro-5-(2-butyl)-4-methyl-4-ethyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
dihydro-5-(2-pentyl)-4,4-dimethyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
dihydro-5-(2-pentyl)-4-methyl-4-propyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
dihydro-5-(3-pentyl)-4,4-dimethyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
dihydro-5-isopropyl-4,4-dimethyl-2,3-furanedione + NADPH
?
-
Substrates: -
Products: -
Products: -
?
ethyl 2-oxopropanoate + NADPH + H+
ethyl (2R)-2-hydroxypropanoate + NADP+
Substrates: 0.496% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
ethyl oxo(phenyl)acetate + NADPH + H+
ethyl (2R)-hydroxy(phenyl)acetate + NADP+
Substrates: 3.45% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
ketopantoyl lactone + NADPH
D-(-)-pantoyl lactone
-
Substrates: and its derivatives
Products: -
Products: -
?
methyl oxo(phenyl)acetate + NADPH + H+
methyl (2R)-hydroxy(phenyl)acetate + NADP+
Substrates: 3.94% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: 100% activity, 99% conversion and more than 99% enantiomeric excess within 5 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: 100% activity, 99% conversion and more than 99% enantiomeric excess within 5 h
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
isatin + NADPH
?
-
Substrates: and its derivatives
Products: -
Products: -
?
methyl 2-oxopropanoate + NADPH + H+
methyl (2R)-2-hydroxypropanoate + NADP+
Substrates: 0.501% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
methyl 2-oxopropanoate + NADPH + H+
methyl (2R)-2-hydroxypropanoate + NADP+
Substrates: 0.501% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
pyridine 3-aldehyde + NADPH + H+
(pyridin-3-yl)methanol + NADP+
Substrates: 0.538% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
pyridine 3-aldehyde + NADPH + H+
(pyridin-3-yl)methanol + NADP+
Substrates: 0.538% activity compared to 2-dehydropantolactone
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not reduce 4-nitrobenzaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not reduce 4-nitrobenzaldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not reduce 4-nitrobenzaldehyde
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: carbonyl reductase specifically catalyzing the reduction of conjugated polyketones
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: carbonyl reductase specifically catalyzing the reduction of conjugated polyketones
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: keto-omega-methylpantoyl lactone is the only analog of ketopantoyl lactone tested that is a substrate
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: keto-omega-methylpantoyl lactone is the only analog of ketopantoyl lactone tested that is a substrate
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: carbonyl reductase specifically catalyzing the reduction of conjugated polyketones
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: several other 2-keto acids
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: several other 2-keto acids
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: ketopantoic acid
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: ketopantoic acid
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: ketopantoic acid
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: ketopantoic acid
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: linear form of oxopantoate
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: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
Substrates: 98% conversion and 99% enantiomeric excess within 2 h
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Substrates: -
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydropantoyl lactone + NADPH
(R)-pantoyl lactone + NADP+
-
Substrates: -
Products: -
Products: -
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
1 mM Ni2+ and Ca2+ have almost no influence over the enzyme activity
additional information
-
1 mM Ni2+ and Ca2+ have almost no influence over the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Polyketones
-
cyclohexenediol-1,2,3,4-tetraone; e.g. parabanic acid
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cataract
Aldo-Keto Reductases: Multifunctional Proteins as Therapeutic Targets in Diabetes and Inflammatory Disease.
Colonic Neoplasms
Inhibition of aldose reductase prevents growth factor-induced G1-S phase transition through the AKT/phosphoinositide 3-kinase/E2F-1 pathway in human colon cancer cells.
Diabetic Nephropathies
Identification of a renal-specific oxido-reductase in newborn diabetic mice.
Diabetic Retinopathy
Aldo-Keto Reductases: Multifunctional Proteins as Therapeutic Targets in Diabetes and Inflammatory Disease.
Neoplasms
Inhibitory effects of polyphenols isolated from Rhus verniciflua on Aldo-keto reductase family 1 B10.
Uveitis
Aldo-Keto Reductases: Multifunctional Proteins as Therapeutic Targets in Diabetes and Inflammatory Disease.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20.4
2-dehydropantolactone
mutant enzyme H128A, at pH 7.0 and 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.01
2-dehydropantolactone
mutant enzyme H128A, at pH 7.0 and 30°C
15.5
2-dehydropantolactone
mutant enzyme T30A, at pH 7.0 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.295
2-dehydropantolactone
mutant enzyme H128A, at pH 7.0 and 30°C
4.43
2-dehydropantolactone
mutant enzyme T30A, at pH 7.0 and 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 5.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
the activity remains above 50% of the maximum activity between 30 and 55°C
35 - 55
between 35 and 55°C, the enzyme activity remains above 70% of the maximal activity
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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.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). B9WJQ5_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
309
0
35183
TrEMBL
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H128A
the mutant shows strongly reduced activity compared to the wild type enzyme
T30A
the mutant shows reduced activity compared to the wild type enzyme
H128A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
T30A
-
the mutant shows reduced activity compared to the wild type enzyme
-
H128A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
T30A
-
the mutant shows reduced activity compared to the wild type enzyme
-
H128A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
T30A
-
the mutant shows reduced activity compared to the wild type enzyme
-
H128A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
T30A
-
the mutant shows reduced activity compared to the wild type enzyme
-
H128A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
T30A
-
the mutant shows reduced activity compared to the wild type enzyme
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
the half-lives of the enzyme are 12.8 and 8.9 h at pH 6.5 and pH 7.0, respectively
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
the residual activity of recombinant enzyme maintains above 90% of the initial activity after 7 h at 30°C. When the enzyme is incubated at 50°C, above 30% of the initial activity still retains after 2 h. The recombinant enzyme exhibits adequate thermal stability, and its half-lives are 45.6, 8.6 and 1.7 h at 30, 40 and 50°C, respectively
40 - 50
the recombinant enzyme exhibits high thermal stability with half-lives of 6.3 h, 3.7 h and 52 min at 40, 45 and 50°C, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
King, H.L.; Wilken, D.R.
Separation and preliminary studies on 2-ketopantoyl lactone and 2-ketopantoic acid reductases of yeast
J. Biol. Chem.
247
4096-4098
1972
Saccharomyces cerevisiae
-
brenda
Wilken, D.R.; King, H.L.; Dyar, R.E.
Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate
J. Biol. Chem.
250
2311-2314
1975
Saccharomyces cerevisiae
brenda
Hata, H.; Shimizu, S.; Hattori, S.; Yamada, H.
Ketopantoyl-lactone reductase is a conjugated polyketone reductase
FEMS Microbiol. Lett.
58
87-90
1989
Saccharomyces cerevisiae
brenda
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
brenda
Wilken, D.R.; Dyar, R.E.
Stereospecificity of pantoyl lactone formed by yeast cells and purified yeast ketopantoyl lactone reductases
Arch. Biochem. Biophys.
189
251-255
1978
Saccharomyces cerevisiae
brenda
Wilken, D.R.; King, H.L.; Dyar, R.E.
Ketopantoyl lactone reductases
Methods Enzymol.
62
209-215
1979
Saccharomyces cerevisiae
brenda
King, H.L.; Dyar, R.E.; Wilken, D.R.
Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase
J. Biol. Chem.
249
4689-4695
1974
Saccharomyces cerevisiae
brenda
Kataoka, M.; Nomura, Y.; Shimizu, S.; Yamada, H.
Enzymes involved in the NADPH regeneration system coupled with asymmetric reduction of carbonyl compounds in microorganisms
Biosci. Biotechnol. Biochem.
56
820-821
1992
Candida parapsilosis, Mucor ambiguus, Mucor ambiguus AKU 3006, Saccharomyces cerevisiae
-
brenda
Julliard, J.H.
Purification and characterization of oxopantoyl lactone reductase from higher plants: role in pantothenate synthesis
Bot. Acta
107
191-200
1994
Spinacia oleracea
-
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 CD36 (B9WJQ5), Candida dubliniensis CD36
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 (H8XA83), Candida orthopsilosis, Candida orthopsilosis 90-125 (H8XA83)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.168)
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