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Information on EC 3.1.1.24 - 3-oxoadipate enol-lactonase
for references in articles please use BRENDA:EC3.1.1.24
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.1 Carboxylic-ester hydrolases
3.1.1.24 3-oxoadipate enol-lactonase
IUBMB Comments
The enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase.
The enzyme appears in viruses and cellular organisms
- 3.1.1.24
- protocatechuate
- acinetobacter
- putida
- calcoaceticus
-
lactonizing
- gamma-carboxymuconolactone
- muconolactone
- catechols
- beta-carboxy-cis,cis-muconate
- dienelactone
-
3,4-dioxygenase
-
succinyl-coenzyme
-
thiolase
-
cycloisomerases
- leguminosarum
-
5.3.3.4
- trifolii
showSynonyms
enol-lactone hydrolase, beta-ketoadipate enol-lactone hydrolase, 3-oxoadipate enol-lactone hydrolase, elh i, elh ii, 3-oxoadipate enol-lactonase, 3-oxoadipate-enol-lactonase, 4-methyl-3-oxoadipate enol-lactone hydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-oxoadipate enol-lactone hydrolase
3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase
EC 3.1.1.24 and EC 4.1.1.44, respectively
beta-ketoadipate enol-lactone hydrolase
carboxymethylbutenolide lactonase
-
-
-
-
EC 3.1.1.16
-
-
formerly, part transferred
-
PcaD
beta-ketoadipate enol-lactone hydrolase
-
form I and II, catD gene product
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
two uptake systems for 4-hydroxybenzoate and protocatechuate by the 3-oxoadipate pathway
-
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
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
-
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
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
-
-
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
4-methylcatechol degradation (ortho cleavage), catechol degradation to beta-ketoadipate, protocatechuate degradation II (ortho-cleavage pathway)
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9031-04-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-oxoadipate-enol-lactone + H2O
3-oxoadipate
Substrates: also known as beta-ketoadipate-enol-lactone
Products: -
Products: -
?
4-hydroxy-3-pentenoic acid gamma-lactone + H2O
4-oxopentanoic acid
Substrates: -
Products: i.e. levulinic acid
Products: i.e. levulinic acid
?
4-methyl-3-oxoadipate enol-lactone + H2O
4-methyl-3-oxoadipate + H+
-
Substrates: -
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
Substrates: 3-oxoadipate enol-lactone
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
Substrates: the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
Substrates: the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
Substrates: the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
Products: -
Products: -
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
Substrates: -
Products: -
Products: -
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme additionally catalyzes the decarboxylation of 4-carboxymuconolactone to give substrate beta-oxoadipate enol-lactone, reaction of EC 4.1.1.44
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme additionally catalyzes the decarboxylation of 4-carboxymuconolactone to give substrate beta-oxoadipate enol-lactone, reaction of EC 4.1.1.44
Products: -
Products: -
?
additional information
?
-
Substrates: PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
Products: -
Products: -
?
additional information
?
-
Substrates: product identification by LC-MS and NMR spectrometric analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: product identification by LC-MS and NMR spectrometric analysis
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
Substrates: the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
Substrates: the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
Products: -
Products: -
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
Substrates: the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
Products: -
Products: -
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
Substrates: -
Products: -
Products: -
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
Products: -
Products: -
?
additional information
?
-
-
Substrates: PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
completely inactivated, activity can not be recovered by adding dithiothreitol
3-oxoadipate
-
50% inhibition at a concentration of 17 mM; i.e. beta-ketoadipate
3-oxoadipate
-
10% inhibition at a concentration of 1 mM; 50% inhibition at a concentration of 10 mM; i.e. beta-ketoadipate
p-chloromercuribenzoate
-
completely inactivated after 49 h at 22°C, activity can not be recovered by adding dithiothreitol
p-chloromercuribenzoate
-
completely inactivated at a concentration of 0.005 mM, 95% of the activity can be recovered by addition of 10 mM dithiothreitol in the reaction mixture; inhibition can not be prevented in the presence of beta-ketoadipate
additional information
-
not inhibited by adipate and levulinate at a concentration of 20 mM
-
additional information
-
not inhibited by adipate and levulinate at a concentration of 20 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 10
7.5 - 10
-
decrease of the activity is dependent on the buffer, the enzyme is less active in Tris-HCl than in potassium phosphate buffer at pH 7.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
biovar trifolii, WU95 wild type, MNF9013 mutant able to grow on protocatechuate, but not on 4-hydroxybenzoate
-
-
brenda
bifunctional 3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase, EC 3.1.1.24 and EC 4.1.1.44, respectively
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
PcaJ (beta-ketoadipate:succinyl-coenzyme A transferase) inactivation results in production of 3-oxoadipate from protocatechuic acid. The mutant is a biocatalyst to produce both 3-oxoadipate and muconolactone from a lignin-related aromatic compound, a portion of the produced 3-oxoadipate is converted to levulinic acid through a purification step consisting of extraction from the culture and recrystallization. Muconolactone is purified from the culture of the PcaD-inactivated mutant of KT2440, although the isomeric beta-ketoadipate enol-lactone is supposed to be produced because it is the substrate of PcaD
malfunction
-
PcaJ (beta-ketoadipate:succinyl-coenzyme A transferase) inactivation results in production of 3-oxoadipate from protocatechuic acid. The mutant is a biocatalyst to produce both 3-oxoadipate and muconolactone from a lignin-related aromatic compound, a portion of the produced 3-oxoadipate is converted to levulinic acid through a purification step consisting of extraction from the culture and recrystallization. Muconolactone is purified from the culture of the PcaD-inactivated mutant of KT2440, although the isomeric beta-ketoadipate enol-lactone is supposed to be produced because it is the substrate of PcaD
-
malfunction
-
PcaJ (beta-ketoadipate:succinyl-coenzyme A transferase) inactivation results in production of 3-oxoadipate from protocatechuic acid. The mutant is a biocatalyst to produce both 3-oxoadipate and muconolactone from a lignin-related aromatic compound, a portion of the produced 3-oxoadipate is converted to levulinic acid through a purification step consisting of extraction from the culture and recrystallization. Muconolactone is purified from the culture of the PcaD-inactivated mutant of KT2440, although the isomeric beta-ketoadipate enol-lactone is supposed to be produced because it is the substrate of PcaD
-
malfunction
-
PcaJ (beta-ketoadipate:succinyl-coenzyme A transferase) inactivation results in production of 3-oxoadipate from protocatechuic acid. The mutant is a biocatalyst to produce both 3-oxoadipate and muconolactone from a lignin-related aromatic compound, a portion of the produced 3-oxoadipate is converted to levulinic acid through a purification step consisting of extraction from the culture and recrystallization. Muconolactone is purified from the culture of the PcaD-inactivated mutant of KT2440, although the isomeric beta-ketoadipate enol-lactone is supposed to be produced because it is the substrate of PcaD
-
metabolism
the enzyme is involved in the protocatechuate branch of the 3-oxoadipate pathway, which is a major pathway involved in the catabolism of the aromatic compounds in microbes
metabolism
the enzyme is part of the metabolic pathway for 4-hydroxphenyl and guaiacyl lignin-related aromatic compounds in Pseudomonas putida strain KT2440. 3-Carboxymuconolactone (CML), muconolactone (ML), and betaketoadipate enol-latone (KEL), i.e. 3-oxoadipate, are intermediates observed in the metabolism of lignin-related aromatics
metabolism
-
the enzyme is part of the metabolic pathway for 4-hydroxphenyl and guaiacyl lignin-related aromatic compounds in Pseudomonas putida strain KT2440. 3-Carboxymuconolactone (CML), muconolactone (ML), and betaketoadipate enol-latone (KEL), i.e. 3-oxoadipate, are intermediates observed in the metabolism of lignin-related aromatics
-
metabolism
-
the enzyme is part of the metabolic pathway for 4-hydroxphenyl and guaiacyl lignin-related aromatic compounds in Pseudomonas putida strain KT2440. 3-Carboxymuconolactone (CML), muconolactone (ML), and betaketoadipate enol-latone (KEL), i.e. 3-oxoadipate, are intermediates observed in the metabolism of lignin-related aromatics
-
metabolism
-
the enzyme is part of the metabolic pathway for 4-hydroxphenyl and guaiacyl lignin-related aromatic compounds in Pseudomonas putida strain KT2440. 3-Carboxymuconolactone (CML), muconolactone (ML), and betaketoadipate enol-latone (KEL), i.e. 3-oxoadipate, are intermediates observed in the metabolism of lignin-related aromatics
-
Show AA Sequence and Transmembrane Helices (351 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000 - 33000
33000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
primarily as dimers, two further bands appear, the protein may associate to form higher oligomers
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
preparation of beta-ketoadipate:succinyl-coenzyme A transferase (PcaJ)- and beta-ketoadipate enol lactone hydrolase (PcaD)-inactivated mutants. A double mutant strain shows no beta-ketoadipate:succinyl-coenzyme A transferase and beta-ketoadipate enol lactone hydrolase activties and is unable to assimilate vanillate (VA) and protocatechuate (PCA), and is designated as Pseudomonas putida strain KT2440-dJ, phenotype, overview
additional information
-
preparation of beta-ketoadipate:succinyl-coenzyme A transferase (PcaJ)- and beta-ketoadipate enol lactone hydrolase (PcaD)-inactivated mutants. A double mutant strain shows no beta-ketoadipate:succinyl-coenzyme A transferase and beta-ketoadipate enol lactone hydrolase activties and is unable to assimilate vanillate (VA) and protocatechuate (PCA), and is designated as Pseudomonas putida strain KT2440-dJ, phenotype, overview
-
additional information
-
preparation of beta-ketoadipate:succinyl-coenzyme A transferase (PcaJ)- and beta-ketoadipate enol lactone hydrolase (PcaD)-inactivated mutants. A double mutant strain shows no beta-ketoadipate:succinyl-coenzyme A transferase and beta-ketoadipate enol lactone hydrolase activties and is unable to assimilate vanillate (VA) and protocatechuate (PCA), and is designated as Pseudomonas putida strain KT2440-dJ, phenotype, overview
-
additional information
-
preparation of beta-ketoadipate:succinyl-coenzyme A transferase (PcaJ)- and beta-ketoadipate enol lactone hydrolase (PcaD)-inactivated mutants. A double mutant strain shows no beta-ketoadipate:succinyl-coenzyme A transferase and beta-ketoadipate enol lactone hydrolase activties and is unable to assimilate vanillate (VA) and protocatechuate (PCA), and is designated as Pseudomonas putida strain KT2440-dJ, phenotype, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
half-life, 3 min in 0.02 M sodium potassium phosphate buffer, pH 6.8, 0.005 mM Mg-EDTA
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
Ni2+ affinity column chromatography and Superdex75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
catD gene cloned and expressed in Pseudomonas putida and Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ornston, L.N.
Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)
Methods Enzymol.
17A
529-549
1970
Pseudomonas putida
-
brenda
Shanley, M.S.; Neidle, E.L.; Parales, R.E.; Ornston, L.N.
Cloning and expression of Acinetobacter calcoaceticus catBCDE genes in Pseudomonas putida and Escherichia coli
J. Bacteriol.
165
557-563
1986
Acinetobacter calcoaceticus
brenda
Ornston, L.N.
The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida
J. Biol. Chem.
241
3787-3794
1966
Pseudomonas putida, Pseudomonas putida A.312
brenda
Wong, C.M.; Dilworth, M.J.; Glenn, A.R.
Evidence for two uptake systems in Rhizobium leguminosarum for hydroxy-aromatic compounds metabolized by the 3-oxoadipate pathway
Arch. Microbiol.
156
385-391
1991
Rhizobium leguminosarum
-
brenda
Eulberg, D.; Lakner, S.; Golovleva, L.A.; Schlmann, M.
Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity
J. Bacteriol.
180
1072-1081
1998
Rhodococcus opacus
brenda
Hughes, E.J.; Shapiro, M.K.; Houghton, J.E.; Ornston, L.N.
Cloning and expression of pca genes from Pseudomomas putida in Escherichia coli
J. Gen. Microbiol.
134
2877-2887
1988
Pseudomonas putida, Pseudomonas putida PRS2000
brenda
Yeh, W.K.; Ornston, L.N.
p-Chloromercuribenzoate specifically modifies thiols associated with the active sites of beta-ketoadipate enol-lactone hydrolase and succinyl CoA: beta-ketoadipate CoA transferase
Arch. Microbiol.
138
102-105
1984
Acinetobacter calcoaceticus, Pseudomonas putida
brenda
Yeh, W.K.; Fletcher, P.; Ornston, L.N.
Evolutionary divergence of co-selected beta-ketoadipate enol-lactone hydrolases in Acinetobacter calcoaceticus
J. Biol. Chem.
255
6342-6346
1980
Acinetobacter calcoaceticus
brenda
McCorkle, G.M.; Yeh, W.K.; Fletcher, P.; Ornston, L.N.
Repetitions in the NH2-terminal amino acid sequence of beta-ketoadipate enol-lactone hydrolase from Pseudomonas putida
J. Biol. Chem.
255
6335-6341
1980
Pseudomonas putida
brenda
Patel, R.N.; Mazumdar, S.; Ornston, L.N.
beta-Ketoadipate enol-lactone hydrolases I and II from Acinetobacter calcoaceticus
J. Biol. Chem.
250
6567-6577
1975
Acinetobacter calcoaceticus
brenda
Marin, M.; Perez-Pantoja, D.; Donoso, R.; Wray, V.; Gonzalez, B.; Pieper, D.H.
Modified 3-oxoadipate pathway for the biodegradation of methylaromatics in Pseudomonas reinekei MT1
J. Bacteriol.
192
1543-1552
2010
Pseudomonas reinekei
brenda
Bains, J.; Kaufman, L.; Farnell, B.; Boulanger, M.J.
A product analog bound form of 3-oxoadipate-enol-lactonase (PcaD) reveals a multifunctional role for the divergent cap domain
J. Mol. Biol.
406
649-658
2011
Paraburkholderia xenovorans (Q13KT2)
brenda
Knapik, A.A.; Petkowski, J.J.; Otwinowski, Z.; Cymborowski, M.T.; Cooper, D.R.; Majorek, K.A.; Chruszcz, M.; Krajewska, W.M.; Minor, W.
A multi-faceted analysis of RutD reveals a novel family of alpha/beta hydrolases
Proteins
80
2359-2368
2012
Paraburkholderia xenovorans (Q13KT2)
brenda
Okamura-Abe, Y.; Abe, T.; Nishimura, K.; Kawata, Y.; Sato-Izawa, K.; Otsuka, Y.; Nakamura, M.; Kajita, S.; Masai, E.; Sonoki, T.; Katayama, Y.
Beta-ketoadipic acid and muconolactone production from a lignin-related aromatic compound through the protocatechuate 3,4-metabolic pathway
J. Biosci. Bioeng.
121
652-658
2016
Pseudomonas putida (Q88N36), Pseudomonas putida ATCC 47054 (Q88N36), Pseudomonas putida DSM 6125 (Q88N36), Pseudomonas putida NCIMB 11950 (Q88N36)
brenda
Yamanashi, T.; Kim, S.Y.; Hara, H.; Funa, N.
In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL the protocatechuate branch of the beta-ketoadipate pathway in Rhodococcus jostii RHA1
Biosci. Biotechnol. Biochem.
79
830-835
2015
Rhodococcus jostii (Q0SH24), Rhodococcus jostii
brenda
EXTERNAL LINKS (specific for EC-Number 3.1.1.24)
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Release 2026.1 (March 2026)
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