Information on EC 1.1.1.358 - 2-dehydropantolactone reductase

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The expected taxonomic range for this enzyme is: Candida parapsilosis

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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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
1-methylisatin + NADPH + H+
?
show the reaction diagram
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86% of the activity compared to isatin
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?
2-dehydropantolactone + NADPH + H+
(R)-pantolactone + NADP+
show the reaction diagram
5-methylisatin + NADPH + H+
?
show the reaction diagram
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108% of the activity compared to isatin
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?
camphorquinone + NADPH + H+
?
show the reaction diagram
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97% of the activity compared to isatin
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-
?
isatin + NADPH + H+
?
show the reaction diagram
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-
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-dehydropantolactone
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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+
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completely inhibits reduction of 2-dehydropantolactone
cyclohexenediol-1,2,3,4-tetraone
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uncompetitive
Hg2+
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completely inhibits reduction of 2-dehydropantolactone
iodoacetate
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1 mM, 49% inhibition
p-chloromercuribenzoate
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0.1 mM, 72% inhibition
parabanic acid
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uncompetitive
quercetin
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0.1 mM, 94% inhibition
Zn2+
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completely inhibits reduction of 2-dehydropantolactone
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085
1-methylisatin
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pH 7.0, 30C
0.333
2-dehydropantolactone
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pH 7.0, 30C
0.016
5-methylisatin
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pH 7.0, 30C
0.014
isatin
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pH 7.0, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
2-dehydropantolactone
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pH 7.0, 30C, substrate: isatin
0.0014
3,4-Dihydroxy-3-cyclobutene-1,2-dione
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pH 7.0, 30C, substrate: isatin
0.0002
cyclohexenediol-1,2,3,4-tetraone
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pH 7.0, 30C, substrate: isatin
3.14
parabanic acid
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pH 7.0, 30C, substrate: isatin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
173
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pH 7.0, 30C, substrate: 2-dehydropantolactone
251
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pH 7.0, 30C, substrate: isatin
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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electrofocussing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
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gel filtration
40000
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polyacrylamide gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with NADPH, sitting drop vapor diffusion method, using 0.1 M TrisHCl (pH 8.1) and 23% (w/v) polyethylene glycol 3350, at 20C
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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
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30C, 30 min, 33% loss of activity
347724
6 - 10
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enzyme is stable
347724
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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pH 7.0, 10 min, 58% loss of activity
60
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pH 7.0, 10 min, 77% loss of activity
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
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4.82% activity compared to the wild type enzyme
F299A
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19.1% activity compared to the wild type enzyme
F300A
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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
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71.1% activity compared to the wild type enzyme
K30A
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55.1% activity compared to the wild type enzyme
K88A
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inactive
R267A
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8.43% activity compared to the wild type enzyme
T27A
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5.75% activity compared to the wild type enzyme
Y63A
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0.17% activity compared to the wild type enzyme
D58A
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4.82% activity compared to the wild type enzyme
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H125A
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1.5% activity compared to the wild type enzyme
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K28A
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71.1% activity compared to the wild type enzyme
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K30A
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55.1% activity compared to the wild type enzyme
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R267A
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8.43% activity compared to the wild type enzyme
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