Information on EC 1.1.1.358 - 2-dehydropantolactone reductase

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The expected taxonomic range for this enzyme is: Candida parapsilosis

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EC NUMBER
COMMENTARY hide
1.1.1.358
-
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RECOMMENDED NAME
GeneOntology No.
2-dehydropantolactone reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+
show the reaction diagram
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phosphopantothenate biosynthesis II
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-
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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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-dehydropantolactone
-
competitive versus isatin
3,4-Dihydroxy-3-cyclobutene-1,2-dione
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uncompetitive
Al3+
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83%% inhibition, reduction of 2-dehydropantolactone
Cd2+
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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
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0.1 mM, 72% inhibition
parabanic acid
-
uncompetitive
quercetin
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0.1 mM, 94% inhibition
Zn2+
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completely inhibits reduction of 2-dehydropantolactone
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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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
2-dehydropantolactone
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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
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pH 7.0, 30°C, substrate: isatin
3.14
parabanic acid
-
pH 7.0, 30°C, substrate: isatin
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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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
electrofocussing
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
gel filtration
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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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
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sitting drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5), 25% (w/v) PEG3350, and 0.2 M NaCl
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sitting drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.1 and 23% (w/v) PEG 3350
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
30°C, 30 min, 33% loss of activity
347724
6 - 10
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enzyme is stable
347724
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni Sepharose column chromatography and Superdex 75 gel filtration
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Ni Sepharose column chromatography, Resource Q column chromatography, and Superdex 75 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
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expressed in Escherichia coli Rosetta(DE3) cells
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ENGINEERING
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
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1.5% activity compared to the wild type enzyme
K264A
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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
K88A
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inactive
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.358)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)