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3-oxoadipate enol-lactone + H2O = 3-oxoadipate
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
two uptake systems for 4-hydroxybenzoate and protocatechuate by the 3-oxoadipate pathway
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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
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-
3-oxoadipate enol-lactone + H2O = 3-oxoadipate
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(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
3-methylmuconolactone + H2O
?
-
-
-
-
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
3-oxoadipate-enol-lactone + H2O
3-oxoadipate
also known as beta-ketoadipate-enol-lactone
-
-
?
4-hydroxy-3-pentenoic acid gamma-lactone + H2O
4-oxopentanoic acid
-
i.e. levulinic acid
-
?
4-methyl-3-oxoadipate enol-lactone + H2O
4-methyl-3-oxoadipate + H+
-
-
-
-
?
additional information
?
-
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate
-
3-oxoadipate enol-lactone
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
?
-
the enzyme acts on the product of EC 4.1.1.44 4-carboxymuconolactone decarboxylase
-
-
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
-
-
-
?
3-oxoadipate enol-lactone + H2O
3-oxoadipate
-
-
-
?
additional information
?
-
enzyme additionally catalyzes the decarboxylation of 4-carboxymuconolactone to give substrate beta-oxoadipate enol-lactone, reaction of EC 4.1.1.44
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the decarboxylation of 4-carboxymuconolactone to give substrate beta-oxoadipate enol-lactone, reaction of EC 4.1.1.44
-
-
?
additional information
?
-
PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
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-
?
additional information
?
-
-
PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
-
-
?
additional information
?
-
product identification by LC-MS and NMR spectrometric analysis
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-
?
additional information
?
-
-
product identification by LC-MS and NMR spectrometric analysis
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-
?
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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
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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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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
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
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 DSM 6125 (Q88N36), Pseudomonas putida NCIMB 11950 (Q88N36), Pseudomonas putida ATCC 47054 (Q88N36)
brenda