Information on EC 3.1.1.24 - 3-oxoadipate enol-lactonase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.24
-
RECOMMENDED NAME
GeneOntology No.
3-oxoadipate enol-lactonase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-methylcatechol degradation (ortho cleavage)
-
-
Benzoate degradation
-
-
catechol degradation to beta-ketoadipate
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
protocatechuate degradation II (ortho-cleavage pathway)
-
-
4-hydroxymandelate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase
The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-04-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A.312
-
-
Manually annotated by BRENDA team
PRS2000
-
-
Manually annotated by BRENDA team
biovar trifolii, WU95 wild type, MNF9013 mutant able to grow on protocatechuate, but not on 4-hydroxybenzoate
-
-
Manually annotated by BRENDA team
erythropolis, 1CP
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
show the reaction diagram
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
show the reaction diagram
3-methylmuconolactone + H2O
?
show the reaction diagram
-
-
-
-
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
show the reaction diagram
-
-
-
-
?
3-oxoadipate-enol-lactone + H2O
3-oxoadipate
show the reaction diagram
also known as beta-ketoadipate-enol-lactone
-
-
?
4-hydroxy-3-pentenoic acid gamma-lactone + H2O
4-oxopentanoic acid
show the reaction diagram
-
i.e. levulinic acid
-
?
4-methyl-3-oxoadipate enol-lactone + H2O
4-methyl-3-oxoadipate + H+
show the reaction diagram
-
-
-
-
?
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
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
show the reaction diagram
3-oxoadipate enol-lactone + H2O
3-oxoadipate
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-oxoadipate
5,5'-dithiobis(2-nitrobenzoic acid)
-
completely inactivated, activity can not be recovered by adding dithiothreitol
p-chloromercuribenzoate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
2-(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10 - 17
3-oxoadipate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.161
-
MNF9013, mutant unable to grow on 4-hydroxybenzoate
0.171
-
WU95, wild type
300
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 10
PDB
SCOP
CATH
ORGANISM
UNIPROT
Paraburkholderia xenovorans (strain LB400)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
-
3 * 11000, SDS-PAGE
12000
-
2 * 12000, SDS-Page
25000
-
ELH I and ELH II, gel filtration
30000 - 33000
42000
-
gel filtration
42230
-
calculated from the DNA sequence
57600
-
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 12000, SDS-Page
homodimer
-
x-ray crystallography
trimer
-
3 * 11000, SDS-PAGE
additional information
-
primarily as dimers, two further bands appear, the protein may associate to form higher oligomers
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with levulinic acid
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
half-life, 3 min in 0.02 M sodium potassium phosphate buffer, pH 6.8, 0.005 mM Mg-EDTA
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
168fold, 6 step purification
-
94fold, 10 step purification
-
can not be separated from 4-carboxymuconolactone decarboxylase, EC 4.1.1.44, which catalyzes the preceding reaction. The gene pcaD, which encodes the 3-oxoadipate enol-lactone hydrolase is fused to a second gene pcaC, which encodes the decarboxylase, a protocatechuate catabolic gene cluster
-
ELH I and II, 290fold, and 550fold
-
Ni2+ affinity column chromatography and Superdex75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catD gene cloned and expressed in Pseudomonas putida and Escherichia coli
-
expressed in Escherichia coli
-
pcaD gene cloned and expressed in Escherichia coli
-
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