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Information on EC 2.8.3.6 - 3-oxoadipate CoA-transferase
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2.8.3.6 3-oxoadipate CoA-transferaseIUBMB Comments
The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate.
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Word Map
- 2.8.3.6
- protocatechuate
-
enol-lactone
-
cycloisomerase
-
3,4-dioxygenase
- gamma-carboxymuconolactone
-
thiolase
- 4-hydroxybenzoate
- trifolii
- leguminosarum
- beta-carboxy-cis,cis-muconate
- calcoaceticus
-
1.13.11.3
- gentisate
- muconate
- rhizobiaceae
- muconolactone
- opacus
The enzyme appears in viruses and cellular organisms
Synonyms
pcaij, beta-ketoadipate succinyl-coenzyme a transferase, 3-oxoadipate coa-transferase, beta-ketoadipate succinyl-coa transferase, beta-ketoadipate:succinyl-coenzyme a transferase, succinyl-coa:3-oxoadipate coa-transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-oxoadipate coenzyme A-transferase
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3-oxoadipate succinyl-CoA transferase
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beta-ketoadipate succinyl-coenzyme A transferase
beta-ketoadipate:succinyl-coenzyme A transferase
coenzyme A-transferase, 3-oxoadipate
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-
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OSC1
PcaIJ
PcaJ
thiophorase beta-ketoadipate succinyl CoA transferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
coenzyme A transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:3-oxoadipate CoA-transferase
The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate.
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CAS REGISTRY NUMBER
COMMENTARY
9026-16-8
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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
succinyl-CoA + 2-oxoadipate
succinate + 2-oxoadipyl-CoA
poor substrate
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-
?
succinyl-CoA + 3-oxoglutarate
succinate + 3-oxoglutaryl-CoA
poor substrate
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-
?
succinyl-CoA + 4-methyl-3-oxoadipate
succinate + 4-methyl-3-oxoadipyl-CoA
poor substrate
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-
?
succinyl-CoA + 3-oxoadipate
?
-
mediates penultimate step in conversion of protocatechuate to succinate and acetyl-CoA via 3-oxoadipate pathway
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-
?
succinyl-CoA + 3-oxoadipate
?
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
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-
?
succinyl-CoA + 3-oxoadipate
?
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
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-
?
succinyl-CoA + 3-oxoadipate
?
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mediates penultimate step in conversion of protocatechuate to succinate and acetyl-CoA via 3-oxoadipate pathway
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?
succinyl-CoA + 3-oxoadipate
?
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together with EC 4.1.1.44 and EC 3.1.1.24 a component of 3-oxoadipate pathway
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-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
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-
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
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-
-
r
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
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-
-
r
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
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r
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
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-
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
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-
-
?
additional information
?
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no substrates are acetoacetate, oxaloacetate or acetyl-CoA, and in the reverse reaction malonate, fumarate, oxalate or acetate
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?
additional information
?
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no substrates are acetoacetate, oxaloacetate or acetyl-CoA, and in the reverse reaction malonate, fumarate, oxalate or acetate
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?
additional information
?
-
no substrates: 2-chloro-3-oxoadpiate, 2-methyl-3-oxoadipate
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-
?
additional information
?
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the enzyme participates in the beta-ketoadipate pathway, overview, expression of the pcaIJF operon is regulated by an IclR-type transcriptional regulator pcaR, whose transcription is negatively autoregulated, and PcaR is a positive regulator of pcaIJF expression and is required for growth of Sinorhizobium meliloti on protocatechuate as the carbon source, pathway overview
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-
?
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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
additional information
?
-
-
the enzyme participates in the beta-ketoadipate pathway, overview, expression of the pcaIJF operon is regulated by an IclR-type transcriptional regulator pcaR, whose transcription is negatively autoregulated, and PcaR is a positive regulator of pcaIJF expression and is required for growth of Sinorhizobium meliloti on protocatechuate as the carbon source, pathway overview
-
-
?
succinyl-CoA + 3-oxoadipate
?
-
mediates penultimate step in conversion of protocatechuate to succinate and acetyl-CoA via 3-oxoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
-
mediates penultimate step in conversion of protocatechuate to succinate and acetyl-CoA via 3-oxoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
-
together with EC 4.1.1.44 and EC 3.1.1.24 a component of 3-oxoadipate pathway
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoadipate
38% inhibition at 2.5 mM, 58% inhibition at 5 mM
adipate
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inhibits the enzyme at concentration above 10 mM, activates at 2 mM
4-chloromercuribenzoate
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modifies selectively cysteinyl side chains at or near the active site, one molecule per alphabeta-protomer inactivates, DTT restores
4-chloromercuribenzoate
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modifies selectively cysteinyl side chains at or near the active site, one molecule per alphabeta-protomer inactivates, DTT restores
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KM VALUE [mM]
SUBSTRATE
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a soil-dwelling bacterium, strain Rm1021, genes SMb20587 and SMb20588, i.e. pcaI and pcaJ
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-
brenda
metagenomic DNA is extracted from the 18 sediment samples from post-monsoon and pre-monsoon Lonar soda lake, India, in 2018 and 2019. Proteobacteria and Firmicutes are prevalent bacterial phyla in the pre-monsoon and post-monsoon samples
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brenda
enzymes from Pseudomonas putida and Acinetobacter are immunologically related, not identical
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brenda
mutant strain ADP152, 2 transferases, I: induced by protocatechuate, II: induced by cis,cis-muconate
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brenda
enzymes from Pseudomonas putida and Acinetobacter are immunologically related, not identical
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the abundant genes for benzoate degradation are pcaI: 3-oxoadipate CoA-transferase, alpha subunit, pcaH: protocatechuate 3,4-dioxygenase, beta subunit, and pcaB: 3-carboxy-cis, cis-muconate cycloisomerase, and 4-oxalocrotonate tautomerase. Comparison of the microbial diversity and functional potential of xenobiotic degradation pathways with seasonal changes in the Lonar soda lake, metagenomic study, overview
metabolism
physiological function
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functional analysis of pre-monsoon and post-monsoon metagenomic samples, overview
Show AA Sequence and Transmembrane Helices (7234 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
?
two non-identical subunits, 25000 Da and 24000 Da, SDS-PAGE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in the absence of sulfhydryl compounds, DTT stabilizes, 80% residual activity after 5h at 0°C in 0.00086 mM DTT
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, in the presence of DTT, 20% loss of activity within 5 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes SMb20587 and SMb20588, i.e. pcaI and pcaJ organized in an operon with a putative beta-ketoadipyl-CoA thiolase gene pcaF, the expression of the pcaIJF operon is regulated by an IclR-type transcriptional regulator, SMb20586, i.e. pcaR, DNA and amino acid sequence determination and analysis, genetic organization and regulation, overview, subcloning and expression of the enzyme in Escherichia coli
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pcaI and pcaJ-genes encoding the two subunits of the enzyme
pcaI and pcaJ-genes encoding the two subunits of the enzyme, expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Katagiri, M.; Hayaishi, O.
Enzymatic degradation of beta-ketoadipic acid
J. Biol. Chem.
226
439-448
1957
Pseudomonas fluorescens, Pseudomonas fluorescens 23
brenda
Yeh, W.K.; Ornston, L.N.
Evolutionarily homologous alpha 2 beta 2 oligomeric structures in beta-ketoadipate succinyl-CoA transferases from Acinetobacter calcoaceticus and Pseudomonas putida
J. Biol. Chem.
256
1565-1569
1981
Acinetobacter calcoaceticus, Pseudomonas putida
brenda
Yeh, W.K.; Ornston, L.N.
Similar structures in gamma-carboxymuconolactone decarboxylase and beta-ketoadipate succinyl coenzyme A transferase
J. Bacteriol.
149
374-377
1982
Pseudomonas putida
brenda
Parales, R.E.; Harwood, C.S.
Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme A transferase in Pseudomonas putida
J. Bacteriol.
174
4657-4666
1992
Pseudomonas putida, Pseudomonas putida (Q01103 and P0A102)
brenda
Gobel, M.; Kassel-Cati, K.; Schmidt, E.; Reineke, W.
Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase
J. Bacteriol.
184
216-223
2002
Pseudomonas knackmussii (Q8VPF3 and Q8VPF2)
brenda
Kaschabek, S.R.; Kuhn, B.; Muller, D.; Schmidt, E.; Reineke, W.
Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase
J. Bacteriol.
184
207-215
2002
Pseudomonas knackmussii (Q8VPF3 and Q8VPF2)
brenda
MacLean, A.M.; MacPherson, G.; Aneja, P.; Finan, T.M.
Characterization of the beta-ketoadipate pathway in Sinorhizobium meliloti
Appl. Environ. Microbiol.
72
5403-5413
2006
Sinorhizobium meliloti
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
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, Pseudomonas putida KT 2240
brenda
Wang, J.; Zhou, L.; Chen, B.; Sun, S.; Zhang, W.; Li, M.; Tang, H.; Jiang, B.; Tang, J.; He, Y.
A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
Sci. Rep.
5
18456
2015
Xanthomonas campestris
brenda
Zeman, I.; Nebohacova, M.; Gerecova, G.; Katonova, K.; Janosikova, E.; Jakubkova, M.; Centarova, I.; Dunckova, I.; Tomaska, L.; Pryszcz, L.P.; Gabaldon, T.; Nosek, J.
Mitochondrial carriers link the catabolism of hydroxyaromatic compounds to the central metabolism in Candida parapsilosis
G3 (Bethesda)
6
4047-4058
2016
Candida parapsilosis, Candida parapsilosis CLIB214
brenda
Chakraborty, J.; Rajput, V.; Sapkale, V.; Kamble, S.; Dharne, M.
Spatio-temporal resolution of taxonomic and functional microbiome of Lonar soda lake of India reveals metabolic potential for bioremediation
Chemosphere
264
128574
2020
uncultured bacterium
brenda
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