We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 1.1.1.358 - 2-dehydropantolactone reductase for references in articles please use BRENDA:EC1.1.1.358
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
conjugated polyketone reductase, conjugated polyketone reductase C2, CPR-C1, CPR-C2, ketopantoyl-lactone reductase, NADPH-dependent ketopantoyl lactone reductase,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
conjugated polyketone reductase C2
-
conjugated polyketone reductase C2
-
-
CPR-C1
-
CPR-C2
-
ketopantoyl-lactone reductase
-
-
ketopantoyl-lactone reductase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Q76L36, Q76L37
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
Q76L36, Q76L37
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
ir
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADPH
-
activity with NADH is 2% compared to the activity with NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
173
-
pH 7.0, 30°C, substrate: 2-dehydropantolactone
251
-
pH 7.0, 30°C, substrate: isatin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CPRC2_CANPA
307
0
34650
Swiss-Prot
CPRC1_CANPA
304
0
34492
Swiss-Prot
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
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 * 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 * 40000, SDS-PAGE
-
monomer
-
1 * 41600, SDS-PAGE
monomer
-
1 * 41600, SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4
-
30°C, 30 min, 33% loss of activity
347724
6 - 10
-
enzyme is stable
347724
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
-
pH 7.0, 10 min, 58% loss of activity
60
-
pH 7.0, 10 min, 77% loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ni Sepharose column chromatography and Superdex 75 gel filtration
-
Ni Sepharose column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
-
expressed in Escherichia coli Rosetta(DE3) cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.1.1.358 2-dehydropantolactone reductase
more
top
Information
