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Information on EC 3.1.1.25 - 1,4-lactonase and Organism(s) Rattus norvegicus and UniProt Accession Q68FP2

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.25 1,4-lactonase
IUBMB Comments
The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q68FP2
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ahl lactonase, ssopox, vmolac, levo-lactonase, vmut_2255, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-lactonase
-
-
-
-
lactonase, gamma
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
1,4-lactone hydroxyacylhydrolase
The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-38-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
show the reaction diagram
-
-
-
?
gamma-butyrolactone + H2O
gamma-hydroxybutyrate
show the reaction diagram
-
-
-
-
r
gamma-caprolactone + H2O
gamma-hydroxycaproate
show the reaction diagram
gamma-octalactone + H2O
4-hydroxyoctanoate
show the reaction diagram
gamma-valerolactone + H2O
gamma-hydroxyvalerate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates, hydrolysis is maximal at 0.01 mM , lactonization is maximal with 10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
eserine
-
weak inhibition
ethanol
-
6%, 85% inhibition
ethyl beta-hydroxybutyrate
-
weak inhibition
Mg2+
-
only inhibition of hydrolytic activity without affecting its lactonizing function
neostigmine
-
-
PCMB
-
0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.748
dihydrocoumarin
pH 7.0, 37°C
6
gamma-butyrolactone
-
-
2.2
Gamma-caprolactone
-
-
140
gamma-hydroxybutyrate
-
-
5.7
Gamma-hydroxycaproate
-
-
20
Gamma-hydroxyvalerate
-
-
3.1
Gamma-octalactone
-
-
4
gamma-valerolactone
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.6
pH 6.0: about 70% of maximal activity, pH 9.6: about 55% of maximal activity, hydrolysis of dihydrocoumarin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 37
-
15°C: about 65% of maximal activity, 37°C: about 90% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
male Wistar rats
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PON3_RAT
354
0
39458
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
almost 100% activity is maintained during the incubation period of 180 min
649767
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 55
180 min, quite stable
60
90 min, 50% loss of activity
90
-
4 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+, 1 mM, stabilizes
-
freezing destroys 30-50% of the activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme is quite stable, showing no decrease in specific activity after storage for 1 month
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the presence of 2.5 mM Ca2+ and 0.1% (w/v) Triton X-100 (as detergent) in the buffers throughout the purification procedure is essential for maintaining the activity of the enzyme. In the absence of calcium and Triton X-100, the enzyme activity is quickly lost
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fishbein, W.N.; Bessman, S.P.
Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of gamma-lactones. I. Tissue localization, stoichiometry, specificity, distinction from esterase
J. Biol. Chem.
241
4835-4841
1966
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Fishbein, W.N.; Bessman, S.P.
Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of gamma-lactones. II. Metal ion effects, kinetics, and equilibria
J. Biol. Chem.
241
4842-4847
1966
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Rodrigo, L.; Gil, F.; Hernandez, A.F.; Lopez, O.; Pla, A.
Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties
Biochem. J.
376
261-268
2003
Rattus norvegicus (Q68FP2)
Manually annotated by BRENDA team