BRENDA - Enzyme Database
show all sequences of 3.1.1.24

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

Yamanashi, T.; Kim, S.Y.; Hara, H.; Funa, N.; Biosci. Biotechnol. Biochem. 79, 830-835 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Rhodococcus jostii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-oxoadipate enol-lactone + H2O
Rhodococcus jostii
-
3-oxoadipate
-
-
?
additional information
Rhodococcus jostii
PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus jostii
Q0SH24
; bifunctional 3-oxoadipate enol-lactone hydrolase/4-carboxymuconolactone decarboxylase, EC 3.1.1.24 and EC 4.1.1.44, respectively
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-oxoadipate enol-lactone + H2O
-
747316
Rhodococcus jostii
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
747316
Rhodococcus jostii
?
-
-
-
-
additional information
PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
747316
Rhodococcus jostii
?
-
-
-
-
additional information
product identification by LC-MS and NMR spectrometric analysis
747316
Rhodococcus jostii
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Rhodococcus jostii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Rhodococcus jostii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-oxoadipate enol-lactone + H2O
Rhodococcus jostii
-
3-oxoadipate
-
-
?
additional information
Rhodococcus jostii
PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-oxoadipate enol-lactone + H2O
-
747316
Rhodococcus jostii
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
747316
Rhodococcus jostii
?
-
-
-
-
additional information
PcaL is a bidomain, bifunctional protein consisting of gamma-carboxy-muconolactone decarboxylase and 3-oxoadipate enol-lactone hydrolase activities
747316
Rhodococcus jostii
?
-
-
-
-
additional information
product identification by LC-MS and NMR spectrometric analysis
747316
Rhodococcus jostii
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Rhodococcus jostii
General Information
General Information
Commentary
Organism
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
Rhodococcus jostii
General Information (protein specific)
General Information
Commentary
Organism
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
Rhodococcus jostii
Other publictions for EC 3.1.1.24
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
751139
Okamura-Abe
Beta-ketoadipic acid and muco ...
Pseudomonas putida, Pseudomonas putida ATCC 47054, Pseudomonas putida DSM 6125, Pseudomonas putida NCIMB 11950
J. Biosci. Bioeng.
121
652-658
2016
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747316
Yamanashi
In vitro reconstitution of th ...
Rhodococcus jostii
Biosci. Biotechnol. Biochem.
79
830-835
2015
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730909
Knapik
A multi-faceted analysis of Ru ...
Paraburkholderia xenovorans
Proteins
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2359-2368
2012
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Bains
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Paraburkholderia xenovorans
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2011
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1
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704325
Marin
Modified 3-oxoadipate pathway ...
Pseudomonas reinekei
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1543-1552
2010
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Eulberg
Characterization of a protocat ...
Rhodococcus opacus
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Wong
-
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Rhizobium leguminosarum
Arch. Microbiol.
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1
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94275
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Cloning and expression of pca ...
Pseudomonas putida, Pseudomonas putida PRS2000
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2877-2887
1988
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2976
Shanley
Cloning and expression of Acin ...
Acinetobacter calcoaceticus
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557-563
1986
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94277
Yeh
p-Chloromercuribenzoate specif ...
Acinetobacter calcoaceticus, Pseudomonas putida
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1984
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Yeh
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Acinetobacter calcoaceticus
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94279
McCorkle
Repetitions in the NH2-termina ...
Pseudomonas putida
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1980
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94280
Patel
beta-Ketoadipate enol-lactone ...
Acinetobacter calcoaceticus
J. Biol. Chem.
250
6567-6577
1975
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2972
Ornston
-
Conversion of catechol and pro ...
Pseudomonas putida
Methods Enzymol.
17A
529-549
1970
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3661
Ornston
The conversion of catechol and ...
Pseudomonas putida, Pseudomonas putida A.312
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241
3787-3794
1966
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