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Information on EC 3.1.1.17 - gluconolactonase
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EC Tree
3.1.1.17 gluconolactonaseIUBMB Comments
Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed separately.
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Word Map
- 3.1.1.17
-
quorum
- lipoprotein
-
calcium-binding
- arylesterase
- hdl
- homoserine
-
ca2+-binding
- calmodulin
-
high-density
-
quorum-sensing
- paraoxonase-1
- phosphotriesterase
-
organophosphate
-
n-acyl
- trifluoperazine
-
organophosphorus
-
quorum-quenching
-
n-acylhomoserine
-
acyl-homoserine
- vanadate
-
hdl-associated
-
subconfluent
-
ef-hand
-
bioscavenger
-
anti-atherogenic
-
androgen-independent
-
l-ascorbic
- pyocyanin
- soman
-
thiolactone
-
ahl-degrading
-
autoinducer
-
zymomonas
- pectobacterium
- phosphothreonine
-
lipoprotein-associated
-
nrk52e
-
glucose-fructose
- synthesis
- analysis
- molecular biology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
regucalcin, lactonase, smp30, senescence marker protein-30, smp30/gnl, human paraoxonase 1, senescence marker protein 30, smp-30, gluconolactonase, aldonolactonase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALase
aldonolactonase
D-glucono-delta-lacton-hydrolase
-
-
-
-
D-glucono-delta-lactone lactonohydrolase
-
-
-
-
EC 3.1.1.18
-
-
formerly
-
GL
glucono-delta-lactonase
GNL
gulonolactonase
-
-
-
-
lactonase
-
-
-
-
membrane-bound D-glucono-delta-lactone hydrolase
MGL
PpgL-like protein
PspL
regucalcin
senescence marker protein-30
SMP30
aldonolactonase
-
-
-
-
GL
-
-
-
-
glucono-delta-lactonase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucono-1,5-lactone + H2O = D-gluconate
-
-
-
-
D-glucono-1,5-lactone + H2O = D-gluconate
Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed as EC 3.1.1.18, aldonolactonase.
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9012-44-6
EC 3.1.1.18
9012-73-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-5-oxo-2-tetrahydrofurancarboxylic acid + H2O
L-alpha-hydroxyglutaric acid
-
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoate
-
hydrolysis: 15 micromol/min/mg
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoate
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hydrolysis: 14.47 micromol/min/mg
-
-
?
L-galactono-1,4-lactone + H2O
?
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-gulono-1,4-lactone + H2O
L-gulonate
wild type enzyme shows 1.24% specific activity, recombinant enzyme shows 105% specific activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
D-galactono-1,4-lactone + H2O
?
wild type enzyme shows 4.33% specific activity, recombinant enzyme shows 70% specific activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
D-galactono-1,4-lactone + H2O
?
wild type enzyme shows 4.33% specific activity, recombinant enzyme shows 70% specific activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
D-glucono-1,4-lactone + H2O
D-gluconate
-
15% of the activity with D-glucono-1,5-lactone
-
-
?
D-glucono-1,4-lactone + H2O
D-gluconate
-
25% of the activity with D-glucono-1,5-lactone
-
-
?
D-glucono-1,5-lactone + H2O
D-gluconate
wild type and recombinant enzyme show 100% specific activity
-
-
r
D-glucono-1,5-lactone + H2O
D-gluconate
wild type and recombinant enzyme show 100% specific activity
-
-
r
D-glucono-1,5-lactone + H2O
D-gluconate
-
100% relative activity
-
-
?
D-glucono-1,5-lactone + H2O
D-gluconate
XC5397 exhibits lactonase activity only toward D-glucono-1,5-lactone
-
-
?
D-glucono-1,5-lactone + H2O
D-gluconate
-
-
-
?
D-gulono-1,4-lactone + H2O
D-galactonate
wild type enzyme shows 12.0% specific activity, recombinant enzyme shows 20.1% specific activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
D-gulono-1,4-lactone + H2O
D-galactonate
wild type enzyme shows 12.0% specific activity, recombinant enzyme shows 20.1% specific activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
D-xylono-1,5-lactone + H2O
D-xylonate
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90% relative activity compared to D-glucono-1,5-lactone
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-
?
D-xylono-1,5-lactone + H2O
D-xylonate
-
90% relative activity compared to D-glucono-1,5-lactone
-
-
?
L-glucono-1,5-lactone + H2O
L-gluconate
wild type enzyme shows 2.49% specific activity, recombinant enzyme shows no activity compared to the reaction with D-glucono-1,5-lactone
-
-
r
L-glucono-1,5-lactone + H2O
L-gluconate
wild type enzyme shows 2.49% specific activity, recombinant enzyme shows no activity compared to the reaction with D-glucono-1,5-lactone
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-
r
additional information
?
-
-
glucose and a high oxygen level are necessary for the induction of the enzyme in the wild-type strain. The goxB mutation results in constitutive expression of all three activities
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-
?
additional information
?
-
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neither beta-glucosidase nor lactonase alone can split cellobionic acid, but when the two enzymes are recombined the cellobionolytic activity is recovered
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-
?
additional information
?
-
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neither beta-glucosidase nor lactonase alone can splitt cellobionic acid, but when the two enzymes are recombined the cellobionolytic activity is revovered
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-
?
additional information
?
-
-
relating lactones rate of hydrolysis reveal an inverse correlation with the docking energy of the ligands-PON1 complex, and a direct correlation with the lactone side chain length
-
-
?
additional information
?
-
-
GNL is a key enzyme involved in vitamin C biosynthesis
-
-
?
additional information
?
-
-
senescence marker protein 30 plays a role in ascorbic acid biosynthesis
-
-
?
additional information
?
-
XC5397 does not hydrolyze D-gulono-1,4-lactone, L-gulono-1,4-lactone, and D-ribono-1,4-lactone
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucono-1,5-lactone + H2O
D-gluconate
-
-
-
?
additional information
?
-
-
glucose and a high oxygen level are necessary for the induction of the enzyme in the wild-type strain. The goxB mutation results in constitutive expression of all three activities
-
-
?
additional information
?
-
-
neither beta-glucosidase nor lactonase alone can splitt cellobionic acid, but when the two enzymes are recombined the cellobionolytic activity is revovered
-
-
?
additional information
?
-
-
GNL is a key enzyme involved in vitamin C biosynthesis
-
-
?
additional information
?
-
-
senescence marker protein 30 plays a role in ascorbic acid biosynthesis
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
the enzyme requires divalent cations such as Mn2+, Mg2+ or Co2+
Mg2+
Mn2+
Zn2+
additional information
Ca2+
-
the purified enzyme is strictly dependent on Ca2+ and undergoes rapid denaturing precipitation on Ca2+ depletion even in the presence of detergent
Mg2+
-
the enzyme requires divalent cations such as Mn2+, Mg2+ or Co2+
Mn2+
-
the enzyme requires divalent cations such as Mn2+, Mg2+ or Co2+
Zn2+
the enzyme requires a divalent metal ion for maximum activity which is obtained by the addition of 0.075 mM Zn2+
additional information
Mn2+, Co2+, Mg2+, and Ca2+ have a significant low effect on the activity to 19, 9, 8, and 7%, respectively
additional information
-
Mn2+, Co2+, Mg2+, and Ca2+ have a significant low effect on the activity to 19, 9, 8, and 7%, respectively
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
EGTA
-
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+
metal-complexing agents
-
activity is restored by excess of Ca2+, Mn2+ or Zn2+
-
EDTA
-
highly sensitive to EDTA, 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+
additional information
not inhibited by L-ascorbic acid and dithiothreitol
-
additional information
-
not inhibited by L-ascorbic acid and dithiothreitol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0162
D-glucono-1,5-lactone
in 1 mM potassium phosphate buffer (pH 7.0) with 0.075 mM CaCl2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE