BRENDA - Enzyme Database show
show all sequences of 3.1.1.24

The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida

Ornston, L.N.; J. Biol. Chem. 241, 3787-3794 (1966)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.012
-
2-(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
Pseudomonas putida
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33000
-
-
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
A.312
-
Pseudomonas putida A.312
-
A.312
-
Purification (Commentary)
Commentary
Organism
422fold
Pseudomonas putida
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
717
-
-
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate enol-lactone
3661
Pseudomonas putida
3-oxoadipate
-
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate enol-lactone
3661
Pseudomonas putida A.312
3-oxoadipate
-
-
-
?
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
55
-
half-life, 3 min in 0.02 M sodium potassium phosphate buffer, pH 6.8, 0.005 mM Mg-EDTA
Pseudomonas putida
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
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
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.012
-
2-(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33000
-
-
Pseudomonas putida
Purification (Commentary) (protein specific)
Commentary
Organism
422fold
Pseudomonas putida
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
717
-
-
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate enol-lactone
3661
Pseudomonas putida
3-oxoadipate
-
-
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O
3-oxoadipate enol-lactone
3661
Pseudomonas putida A.312
3-oxoadipate
-
-
-
?
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
55
-
half-life, 3 min in 0.02 M sodium potassium phosphate buffer, pH 6.8, 0.005 mM Mg-EDTA
Pseudomonas putida
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
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
Pseudomonas putida
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)
747316
Yamanashi
In vitro reconstitution of th ...
Rhodococcus jostii
Biosci. Biotechnol. Biochem.
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830-835
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730909
Knapik
A multi-faceted analysis of Ru ...
Paraburkholderia xenovorans
Proteins
80
2359-2368
2012
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715929
Bains
A product analog bound form of ...
Paraburkholderia xenovorans
J. Mol. Biol.
406
649-658
2011
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1
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2
1
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704325
Marin
Modified 3-oxoadipate pathway ...
Pseudomonas reinekei
J. Bacteriol.
192
1543-1552
2010
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2
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33102
Eulberg
Characterization of a protocat ...
Rhodococcus opacus
J. Bacteriol.
180
1072-1081
1998
-
-
-
-
-
-
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2
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3
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1
1
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2
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3671
Wong
-
Evidence for two uptake system ...
Rhizobium leguminosarum
Arch. Microbiol.
156
385-391
1991
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94275
Hughes
Cloning and expression of pca ...
Pseudomonas putida, Pseudomonas putida PRS2000
J. Gen. Microbiol.
134
2877-2887
1988
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1
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2
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4
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4
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1
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4
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2976
Shanley
Cloning and expression of Acin ...
Acinetobacter calcoaceticus
J. Bacteriol.
165
557-563
1986
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1
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1
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1
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5
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2
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1
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1
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1
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2
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94277
Yeh
p-Chloromercuribenzoate specif ...
Acinetobacter calcoaceticus, Pseudomonas putida
Arch. Microbiol.
138
102-105
1984
-
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7
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2
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5
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4
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7
2
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2
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4
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94278
Yeh
Evolutionary divergence of co- ...
Acinetobacter calcoaceticus
J. Biol. Chem.
255
6342-6346
1980
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1
1
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5
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1
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1
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94279
McCorkle
Repetitions in the NH2-termina ...
Pseudomonas putida
J. Biol. Chem.
255
6335-6341
1980
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2
1
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6
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1
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1
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1
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1
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94280
Patel
beta-Ketoadipate enol-lactone ...
Acinetobacter calcoaceticus
J. Biol. Chem.
250
6567-6577
1975
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2
1
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5
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1
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2
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2
2
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1
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1
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2
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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
J. Biol. Chem.
241
3787-3794
1966
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1
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1
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2
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1
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1
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