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Information on EC 1.1.1.358 - 2-dehydropantolactone reductase and Organism(s) Candida parapsilosis and UniProt Accession Q76L36

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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).
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Candida parapsilosis
UNIPROT: Q76L36
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The taxonomic range for the selected organisms is: Candida parapsilosis
The expected taxonomic range for this enzyme is: Saccharomycetales
Synonyms
cpr-01, ketopantoyl-lactone reductase, corcpr, cducpr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
conjugated polyketone reductase
-
conjugated polyketone reductase C2
-
CPR-C2
NADPH-dependent ketopantoyl lactone reductase
-
conjugated polyketone reductase
-
ketopantoyl-lactone reductase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
1-methylisatin + NADPH + H+
?
show the reaction diagram
-
86% of the activity compared to isatin
-
-
?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
5-methylisatin + NADPH + H+
?
show the reaction diagram
-
108% of the activity compared to isatin
-
-
?
camphorquinone + NADPH + H+
?
show the reaction diagram
-
97% of the activity compared to isatin
-
-
?
isatin + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
173
-
pH 7.0, 30°C, substrate: 2-dehydropantolactone
251
-
pH 7.0, 30°C, substrate: isatin
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
electrofocussing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CPRC2_CANPA
307
0
34650
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34650
x * 34650, isoform CPR-C2, calculated from amino acid sequence
36000
x * 36000, isoform CPR-C2, SDS-PAGE
40000
x * 40000, SDS-PAGE
31000
-
gel filtration
34491
x * 34491, isoform CPR-C1, calculated from amino acid sequence
38000
x * 38000, isoform CPR-C1, SDS-PAGE
40000
-
polyacrylamide gel electrophoresis
41600
-
1 * 41600, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 41600, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
30°C, 30 min, 33% loss of activity
347724
6 - 10
-
enzyme is stable
347724
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
pH 7.0, 10 min, 58% loss of activity
60
-
pH 7.0, 10 min, 77% loss of activity
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team