Information on EC 2.8.3.6 - 3-oxoadipate CoA-transferase

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The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY
2.8.3.6
-
RECOMMENDED NAME
GeneOntology No.
3-oxoadipate CoA-transferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
coenzyme A transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
3-oxoadipate degradation
-
4-methylcatechol degradation (ortho cleavage)
-
Benzoate degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:3-oxoadipate CoA-transferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-oxoadipate coenzyme A-transferase
-
-
-
-
3-oxoadipate succinyl-CoA transferase
-
-
-
-
3-oxoadipate:succinyl-coenzyme A transferase
-
-
beta-ketoadipate succinyl-CoA transferase
-
-
beta-ketoadipate succinyl-coenzyme A transferase
-
-
coenzyme A-transferase, 3-oxoadipate
-
-
-
-
thiophorase beta-ketoadipate succinyl CoA transferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-16-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzymes from Pseudomonas putida and Acinetobacter are immunologically related, not identical
-
-
Manually annotated by BRENDA team
mutant strain ADP152, 2 transferases, I: induced by protocatechuate, II: induced by cis,cis-muconate
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens 23
strain 23
-
-
Manually annotated by BRENDA team
-
Q8VPF3 and Q8VPF2
UniProt
Manually annotated by BRENDA team
-
Q01103 and P0A102
UniProt
Manually annotated by BRENDA team
enzymes from Pseudomonas putida and Acinetobacter are immunologically related, not identical; strains PRS 2260
-
-
Manually annotated by BRENDA team
PRS2000 (wild-type), PRS2241(pHRP100) or PRS3004(pHRP100)
-
-
Manually annotated by BRENDA team
Pseudomonas reinekei MT1
-
-
-
Manually annotated by BRENDA team
a soil-dwelling bacterium, strain Rm1021, genes SMb20587 and SMb20588, i.e. pcaI and pcaJ
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + 2-oxoadipate
succinate + 2-oxoadipyl-CoA
show the reaction diagram
-
poor substrate
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
-
-
-
r
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
-
-
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
Q01103 and P0A102
-
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
-
-
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
-, Q01103 and P0A102
-
-
-
-
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
-
-
-
r
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
Pseudomonas reinekei, Pseudomonas reinekei MT1
-
-
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
Pseudomonas fluorescens 23
-
-
-
r
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-, Q01103 and P0A102
-
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-, Q01103 and P0A102
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
Q8VPF3 and Q8VPF2
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-
mediates penultimate step in conversion of protocatechuate to succinate and acetyl-CoA via 3-oxoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-
together with EC 4.1.1.44 and EC 3.1.1.24 a component of 3-oxoadipate pathway
-
-
?
succinyl-CoA + 3-oxoglutarate
succinate + 3-oxoglutaryl-CoA
show the reaction diagram
-
poor substrate
-
-
?
succinyl-CoA + 4-methyl-3-oxoadipate
succinate + 4-methyl-3-oxoadipyl-CoA
show the reaction diagram
-
poor substrate
-
-
?
3-oxoadipate + succinyl-CoA
3-oxoadipyl-CoA + succinate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no substrates are acetoacetate, oxaloacetate or acetyl-CoA, and in the reverse reaction malonate, fumarate, oxalate or acetate
-
-
-
additional information
?
-
-
no substrates: 2-chloro-3-oxoadpiate, 2-methyl-3-oxoadipate
-
-
-
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
-
-
-
additional information
?
-
Pseudomonas fluorescens 23
-
no substrates are acetoacetate, oxaloacetate or acetyl-CoA, and in the reverse reaction malonate, fumarate, oxalate or acetate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
-
-
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-, Q01103 and P0A102
-
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-, Q01103 and P0A102
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
Q8VPF3 and Q8VPF2
penultimate step in conversion of benzoate and 4-hydroxybenzoate to tricarboxylic acid cycle intermediates utilizing the beta-ketoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-
mediates penultimate step in conversion of protocatechuate to succinate and acetyl-CoA via 3-oxoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
?
show the reaction diagram
-
together with EC 4.1.1.44 and EC 3.1.1.24 a component of 3-oxoadipate pathway
-
-
?
succinyl-CoA + 3-oxoadipate
succinate + 3-oxoadipyl-CoA
show the reaction diagram
Pseudomonas reinekei MT1
-
-
-
-
?
3-oxoadipate + succinyl-CoA
3-oxoadipyl-CoA + succinate
show the reaction diagram
-
-
-
-
?
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoadipate
-
38% inhibition at 2.5 mM, 58% inhibition at 5 mM
4-chloromercuribenzoate
-
modifies selectively cysteinyl side chains at or near the active site, one molecule per alphabeta-protomer inactivates, DTT restores
Adipate
-
inhibits the enzyme at concentration above 10 mM, activates at 2 mM
NADH
-
28% inhibition at 0.8 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
3-Oxoadipate
-
pH 8, 25C
0.2
-
succinyl-CoA
-
pH 8, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
-
-
crude extract
24.2
-
-
transferase I
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
23
-
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas fluorescens 23
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
108000
-
-
gel filtration
109000
-
-
gel filtration
115000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
two non-identical subunits
tetramer
-
alpha2beta2, 2 * 25600 + 2 * 26500, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 24200 + 2 * 25300, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 32900 + 2 * 27000, SDS-PAGE
?
-, Q01103 and P0A102
; two non-identical subunits, 25000 Da and 24000 Da, SDS-PAGE
additional information
-
amino acid composition
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
1 h, stable in the presence of DTT
40
45
-
30 min, stable
40
-
-
t1/2: 26 min
45
-
-
t1/2: 4 min
50
-
-
30 min, 10% loss of activity
50
-
-
t1/2: 1 min
60
-
-
10 min, stable at neutral pH
80
-
-
5 min, inactivation at neutral pH
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable for 1h at 22C in the presence of 0.00092 mM DTT
-
unstable in the absence of sulfhydryl compounds, DTT stabilizes, 80% residual activity after 5h at 0C in 0.00086 mM DTT
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, in the presence of DTT, 20% loss of activity within 5 h
-
-10C, at least 3 months
-
0C, in the presence of DTT, 20% loss of activity within 5 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-, Q01103 and P0A102
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
-