Information on EC 3.1.1.17 - gluconolactonase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.1.17
-
RECOMMENDED NAME
GeneOntology No.
gluconolactonase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucono-1,5-lactone + H2O = D-gluconate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Entner-Doudoroff pathway II (non-phosphorylative)
-
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
-
glucose and glucose-1-phosphate degradation
-
-
glucose degradation (oxidative)
-
-
L-ascorbate biosynthesis IV
-
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L-ascorbate biosynthesis VI (engineered pathway)
-
-
sorbitol biosynthesis II
-
-
ascorbate metabolism
-
-
Entner Doudoroff pathway
-
-
Pentose phosphate pathway
-
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Ascorbate and aldarate metabolism
-
-
Caprolactam degradation
-
-
Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
D-glucono-1,5-lactone lactonohydrolase
Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed separately.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-44-6
EC 3.1.1.18
9012-73-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme is involved in ascorbic acid biosynthesis
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,5S)-oxabicyclooctenone + H2O
?
show the reaction diagram
-
hydrolysis: 0.83 micromol/min/mg
-
-
?
(1S,5R)-oxabicyclooctenone + H2O
?
show the reaction diagram
-
hydrolysis: 1.67 micromol/min/mg
-
-
?
(S)-5-oxo-2-tetrahydrofurancarboxylic acid + H2O
L-alpha-hydroxyglutaric acid
show the reaction diagram
-
-
-
-
?
6-phosphoglucono-1,5-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-angelica lactone + H2O
?
show the reaction diagram
-
hydrolysis: 18.3 micromol/min/mg
-
-
?
beta-hydroxybutyrolactone + H2O
?
show the reaction diagram
-
hydrolysis: 3.83 micromol/min/mg
-
-
?
D-cellobiono-1,5-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
D-galactonic acid + H2O
?
show the reaction diagram
D-galactono-1,4-lactone + H2O
?
show the reaction diagram
D-galactono-1,4-lactone + H2O
biono-1,5-lactone
show the reaction diagram
-
-
-
-
?
D-galactono-1,5-lactone + H2O
D-galactonate
show the reaction diagram
-
-
-
-
?
D-glucono-1,4-lactone + H2O
D-gluconate
show the reaction diagram
D-glucono-1,5-lactone + H2O
D-gluconate
show the reaction diagram
D-gulono-1,4-lactone + H2O
D-galactonate
show the reaction diagram
D-gulono-1,5-lactone + H2O
?
show the reaction diagram
-
-
-
?
D-gulono-1,5-lactone + H2O
D-gulonate
show the reaction diagram
-
-
-
-
?
D-xylono-1,5-lactone + H2O
D-xylonate
show the reaction diagram
delta-decanolactone + H2O
?
show the reaction diagram
-
hydrolysis: 25.1 micromol/min/mg
-
-
?
delta-dodecanolactone + H2O
?
show the reaction diagram
-
hydrolysis: 9.65 micromol/min/mg
-
-
?
delta-hexalactone + H2O
?
show the reaction diagram
-
hydrolysis: 7.2 micromol/min/mg
-
-
?
delta-nonalactone + H2O
?
show the reaction diagram
-
hydrolysis: 15 micromol/min/mg
-
-
?
delta-undecatiolactone + H2O
?
show the reaction diagram
-
hydrolysis: 28.7 micromol/min/mg
-
-
?
delta-valerolactone + H2O
?
show the reaction diagram
-
hydrolysis: 67.1 micromol/min/mg
-
-
?
dihydrocoumarin + H2O
?
show the reaction diagram
-
hydrolysis: 12.99 micromol/min/mg
-
-
?
epsilon-caprolactone + H2O
?
show the reaction diagram
-
hydrolysis: 14.8 micromol/min/mg
-
-
?
gamma-butyrolactone + H2O
?
show the reaction diagram
-
hydrolysis: 3.21 micromol/min/mg
-
-
?
gamma-decalactone + H2O
?
show the reaction diagram
-
hydrolysis: 17.38 micromol/min/mg
-
-
?
gamma-heptalactone + H2O
?
show the reaction diagram
-
hydrolysis: 5.72 micromol/min/mg
-
-
?
gamma-hexalactone + H2O
?
show the reaction diagram
-
hydrolysis: 5.17 micromol/min/mg
-
-
?
gamma-nonalactone + H2O
?
show the reaction diagram
-
hydrolysis: 14.47 micromol/min/mg
-
-
?
gamma-octalactone + H2O
?
show the reaction diagram
-
hydrolysis: 6.92 micromol/min/mg
-
-
?
gamma-undecalactone + H2O
?
show the reaction diagram
-
hydrolysis: 12.72 micromol/min/mg
-
-
?
gamma-valerolactone + H2O
?
show the reaction diagram
-
hydrolysis: 4.5 micromol/min/mg
-
-
?
homogenestic acid lactone + H2O
?
show the reaction diagram
-
hydrolysis: 32.95 micromol/min/mg
-
-
?
L-galactono-1,4-lactone + H2O
?
show the reaction diagram
wild type enzyme shows 0.37% specific activity, recombinant enzyme shows 62.8% specific activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
L-galactono-1,5-lactone + H2O
L-galactonate
show the reaction diagram
-
-
-
-
?
L-glucono-1,5-lactone + H2O
L-gluconate
show the reaction diagram
L-gulonic acid + H2O
?
show the reaction diagram
-
-
-
?
L-gulono-1,4-lactone + H2O
L-gulonate
show the reaction diagram
wild type enzyme shows 1.24% specific activity, recombinant enzyme shows 105% specific activity compared to the reaction with D-glucono-1,5-lactone
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-
r
L-gulono-1,5-lactone + H2O
L-gulonate
show the reaction diagram
-
-
-
-
?
lactabionic-1,5-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
phenyl acetate + H2O
?
show the reaction diagram
-
hydrolysis: 112 micromol/min/mg
-
-
?
valerolactone + H2O
?
show the reaction diagram
-
-
-
-
?
xylitol + H2O
?
show the reaction diagram
additional information
?
-
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
D-glucono-1,5-lactone + H2O
D-gluconate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
the enzyme requires divalent cations such as Mn2+, Mg2+ or Co2+
Zinc
-
contains at least 1 atom of tightly bound zinc per enzyme subunit
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate/Cu2+
-
oxidative system ascorbate/Cu2+ is the most potent in inactivating the lactonase activity of purified PON1, 0.5 mM/0.001 mM: up to 100% inhibition, 0.1 mM/0.001 mM: 90% inhibition, 95%-100% inhibition. Oleic acid prevents the ascorbate/Cu2+-induced inactivation
ascorbate/Fe2+
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0.5 mM/0.002 mM: 20% inhibiiton
Cu2+
-
0.001 mM, 30% inhibition
Diazotetrazole
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EGTA
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highly sensisitve to EGTA, the lost activity can be restored to the original level by the addition of divalent cations of the order Ca2+ = Mg2+ > Zn2+ > Fe2+ = Co2+, Mn2+, Ni2+, Cu2+ > Mo2+
ethanol
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10 mM, 20% inhibition
metal-complexing agents
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activity is restored by excess of Ca2+, Mn2+ or Zn2+
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N-Acetylimidazole
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N-ethylmaleimide
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NaOCl
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1 mM, 20% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydrogen peroxide
stimulates activity at 0.1-0.5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0162 - 25
D-glucono-1,5-lactone
2.08
D-gulono-1,5-lactone
recombinant enzyme
6.2
glucono-1,5-lactone
-
-
1.55
L-galactonic acid
recombinant enzyme
1.67
L-galactono-1,4-lactone
recombinant enzyme
4.55
L-Gulonic acid
recombinant enzyme
3.05
L-gulono-1,4-lactone
recombinant enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
192
D-glucono-1,5-lactone
wild type enzyme
160
D-gulono-1,5-lactone
recombinant enzyme
615
L-galactonic acid
recombinant enzyme
450
L-galactono-1,4-lactone
recombinant enzyme
1503
L-Gulonic acid
recombinant enzyme
1040
L-gulono-1,4-lactone
recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
-
crude extract
0.8
wild type enzyme, using L-galactono-1,4-lactone as substrate
2.5
-
after 31.2fold purification
2.7
wild type enzyme, using L-gulono-1,4-lactone as substrate
5.4
wild type enzyme, using L-glucono-1,5-lactone as substrate
9.4
wild type enzyme, using D-galactono-1,4-lactone as substrate
12
wild type enzyme, using D-gulono-1,4-lactone as substrate
20.1
recombinant enzyme, using D-gulono-1,4-lactone as substrate
24.5
recombinant enzyme, using L-galactono-1,4-lactone as substrate
27.3
recombinant enzyme, using D-galactono-1,4-lactone as substrate
39
recombinant enzyme, using D-glucono-1,5-lactone as substrate
40.9
recombinant enzyme, using L-gulono-1,4-lactone as substrate
217
wild type enzyme, using D-glucono-1,5-lactone as substrate
1001
-
-
1040
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
-
8.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
additional information
-
not detected in spleen
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
3 * 30000 or 4 * 44000, SDS-PAGE
32000
-
2 * 32000, SDS-PAGE
37200
-
6 * 37200, SDS-PAGE
39400
-
6 * 39400, SDS-PAGE
40000
-
about 40000 Da, SDS-PAGE
44000
-
3 * 30000 or 4 * 44000, SDS-PAGE
45000
-
SDS-PAGE
60000
-
2 * 60000, gel filtration and SDS-PAGE
63000
-
gel filtration
90000
-
gel filtration
120000
-
gel filtration
223000
-
gel filtration
233000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 32000, SDS-PAGE
hexamer
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-dop vapor diffusion method, using 28% (w/v) PEG6000, 100 mM Tris-HCl pH 7.5, and 5 mM CaCl2
hanging drop vapor diffusion method, using 1.6 M ammonium sulfate and 100 mM Tris-HCl, pH 8.5
sitting drop vapour diffusion method, using 0.1 M imidazole (pH 8.0), 0.25 M Ca(OAc)2, and 15% PEG 3350 as a precipitant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
in presence of 0.1% Tween 20 and 5 mM dithiothreitol, half-life: 5 days
25
-
in presence of 0.1% Tween 20 and 5 mM dithiothreitol, half-life: 35 days
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
100 mM NaCl, 4 mM K-gluconate or 25% glycerol slightly stabilize
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Toyopearl DEAE-650M column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
His-Trap nickel affinity chromatography column chromatography and Superdex 75 gel filtration
-
polyethyleneglycol 6000 precipitation and Sephadex G-75 gel filtration
-
TALON metal affinity resin column chromatography
Toyopearl DEAE-650M column chromatography, Toyopearl SuperQ-650M column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
using different types of chromatographies
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) pLysS cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)-Rossetta2/pLysS cells
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
expression in Escherichia coli
-
expression in Escherichia coli JM101
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SMP30/GNL mRNA expression is evident at the start of gestation, increases for the next 8 days then decreases rapidly until day 11 of gestation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E48A
mutant shows only marginal activities of approximately 10% toward D-glucono-1,5-lactone compared to that of the wild type enzyme
N134A
mutant shows only marginal activities of approximately 10% toward D-glucono-1,5-lactone compared to that of the wild type enzyme
N191
mutant shows only marginal activities of approximately 10% toward D-glucono-1,5-lactone compared to that of the wild type enzyme
synthesis
-
the enzyme is useful in the enzymatic bioconversion of fructose and lactose to gluconic acid and sorbitol, respectively, by the enzyme's glucose-fructose oxidoreductase and gluconolactonase activities, method development and evaluation for separation of reaction product mixtures containing lactobionic acid, sorbitol, lactose and fructose by HPLC, overview
additional information
-
SMP30/GNL knockout mice lack the ability to synthesize vitamin C in vivo
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
molecular biology
-
coimmobilization with glucose oxidase in polyelectrolyte gels for improvement of kinetic properties, active enzymes in the gel undergo a shrinking process due to a sudden drop in pH, gel volume phase transition, overview
synthesis
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