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EC Tree
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).
Word Map
1.1.1.358
sirtuins
deacetylation
histone
resveratrol
nad+-dependent
nicotinamide
longevity
nad+
lifespan
sirt1-mediated
calorie
sirtinol
sirts
high-fat
proliferator-activated
cardiomyocytes
mating
forkhead
sirt1-dependent
cr
diet-induced
caspase-3
polyphenolic
foxo3a
anti-aging
amp-activated
hdacs
senescence-associated
aging-associated
srebp-1c
cardioprotective
aging-related
mating-type
dinucleotide-dependent
sirt1-7
coactivator-1
hyperacetylation
resveratrol-induced
mir-34a
nafld
non-histone
pgc-1alpha
nampt
The expected taxonomic range for this enzyme is: Candida parapsilosis
Synonyms
ketopantoyl-lactone reductase,
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conjugated polyketone reductase
conjugated polyketone reductase C2
ketopantoyl-lactone reductase
NADPH-dependent ketopantoyl lactone reductase
-
conjugated polyketone reductase
-
conjugated polyketone reductase
-
conjugated polyketone reductase
-
conjugated polyketone reductase C2
-
conjugated polyketone reductase C2
-
CPR-C1
-
CPR-C2
-
ketopantoyl-lactone reductase
-
-
ketopantoyl-lactone reductase
-
-
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(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
-
-
-
-
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(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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1-methylisatin + NADPH + H+
?
-
86% of the activity compared to isatin
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
5-methylisatin + NADPH + H+
?
-
108% of the activity compared to isatin
-
?
camphorquinone + NADPH + H+
?
-
97% of the activity compared to isatin
-
?
isatin + NADPH + H+
?
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
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
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
ir
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+
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
?
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NADPH
-
NADPH
-
activity with NADH is 2% compared to the activity with NADPH
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2-dehydropantolactone
-
competitive versus isatin
3,4-Dihydroxy-3-cyclobutene-1,2-dione
-
uncompetitive
Al3+
-
83%% inhibition, reduction of 2-dehydropantolactone
Cd2+
-
97% inhibition, reduction of 2-dehydropantolactone
Cu2+
-
completely inhibits reduction of 2-dehydropantolactone
cyclohexenediol-1,2,3,4-tetraone
-
uncompetitive
Hg2+
-
completely inhibits reduction of 2-dehydropantolactone
iodoacetate
-
1 mM, 49% inhibition
p-chloromercuribenzoate
-
0.1 mM, 72% inhibition
parabanic acid
-
uncompetitive
quercetin
-
0.1 mM, 94% inhibition
Zn2+
-
completely inhibits reduction of 2-dehydropantolactone
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0.085
1-methylisatin
-
pH 7.0, 30°C
0.333
2-dehydropantolactone
-
pH 7.0, 30°C
0.016
5-methylisatin
-
pH 7.0, 30°C
0.014
isatin
-
pH 7.0, 30°C
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0.19
2-dehydropantolactone
-
pH 7.0, 30°C, substrate: isatin
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
3.14
parabanic acid
-
pH 7.0, 30°C, substrate: isatin
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173
-
pH 7.0, 30°C, substrate: 2-dehydropantolactone
251
-
pH 7.0, 30°C, substrate: isatin
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-
-
-
brenda
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SwissProt
brenda
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SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
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CPRC2_CANPA
307
0
34650
Swiss-Prot
other Location (Reliability: 4 )
CPRC1_CANPA
304
0
34492
Swiss-Prot
other Location (Reliability: 2 )
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34491
x * 34491, isoform CPR-C1, calculated from amino acid sequence
34650
x * 34650, isoform CPR-C2, calculated from amino acid sequence
36000
x * 36000, isoform CPR-C2, SDS-PAGE
38000
x * 38000, isoform CPR-C1, SDS-PAGE
41600
-
1 * 41600, SDS-PAGE
40000
-
polyacrylamide gel electrophoresis
40000
x * 40000, SDS-PAGE
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?
x * 40000, SDS-PAGE
?
x * 34491, isoform CPR-C1, calculated from amino acid sequence
?
x * 34650, isoform CPR-C2, calculated from amino acid sequence
?
x * 36000, isoform CPR-C2, SDS-PAGE
?
x * 38000, isoform CPR-C1, SDS-PAGE
?
-
x * 34650, isoform CPR-C2, calculated from amino acid sequence
?
-
x * 36000, isoform CPR-C2, SDS-PAGE
?
-
x * 34491, isoform CPR-C1, calculated from amino acid sequence
?
-
x * 38000, isoform CPR-C1, SDS-PAGE
monomer
-
1 * 41600, SDS-PAGE
monomer
-
1 * 41600, SDS-PAGE
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apoenzyme and in complex with NADPH, sitting drop vapor diffusion method, using 0.1 M Tris–HCl (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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D58A
4.82% activity compared to the wild type enzyme
F299A
19.1% activity compared to the wild type enzyme
F300A
17.8% activity compared to the wild type enzyme
H125A
1.5% activity compared to the wild type enzyme
K264A
65.7% activity compared to the wild type enzyme
K28A
71.1% activity compared to the wild type enzyme
K30A
55.1% activity compared to the wild type enzyme
R267A
8.43% activity compared to the wild type enzyme
T27A
5.75% activity compared to the wild type enzyme
Y63A
0.17% activity compared to the wild type enzyme
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4
-
30°C, 30 min, 33% loss of activity
347724
6 - 10
-
enzyme is stable
347724
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40
-
pH 7.0, 10 min, 58% loss of activity
60
-
pH 7.0, 10 min, 77% loss of activity
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Ni Sepharose column chromatography and Superdex 75 gel filtration
Ni Sepharose column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
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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 (Q76L36), Candida parapsilosis (Q76L37), Candida parapsilosis IFO 0708 (Q76L36), Candida parapsilosis IFO 0708 (Q76L37)
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
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1.1.1.358 2-dehydropantolactone reductase
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