BRENDA - Enzyme Database show
show all sequences of 5.3.2.6

Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase

Whitman, C.; Hajipour, G.; Watson, R.; Johnson Jr., W.; Bembenek, M.; Stolowich, N.; J. Am. Chem. Soc. 114, 10104-10110 (1992)
No PubMed abstract available

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14000
-
x * 14000, 5-(carboxymethyl)-2-hydroxymuconate isomerase, SDS-PAGE
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Escherichia coli C
-
-
-
Pseudomonas putida
-
-
-
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
-
-
Purification (Commentary)
Commentary
Organism
native enzyme from Escherichia coli strain C by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, ultrafiltration, ammoniums ulfate fractionation, and hydrophobic interaction chromatography, followed by gel filtration
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxymuconate
stereospecific ketonization
719634
Pseudomonas putida
2-oxo-3-(E)-hexenedioate
-
-
-
?
2-hydroxymuconate
stereospecific ketonization, a reaction of EC 5.3.2.6, is also catalyzed by 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10
719634
Escherichia coli
2-oxo-3-(E)-hexenedioate
-
-
-
?
2-hydroxymuconate
stereospecific ketonization
719634
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3-(E)-hexenedioate
-
-
-
?
2-hydroxymuconate
stereospecific ketonization, a reaction of EC 5.3.2.6, is also catalyzed by 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10
719634
Escherichia coli C
2-oxo-3-(E)-hexenedioate
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 14000, 5-(carboxymethyl)-2-hydroxymuconate isomerase, SDS-PAGE
Escherichia coli
?
x * 3600, 4-oxalocrotonate tautomerase, SDS-PAGE
Pseudomonas putida
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
30
-
assay at
Pseudomonas putida
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Escherichia coli
7.3
-
assay at
Pseudomonas putida
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
14000
-
x * 14000, 5-(carboxymethyl)-2-hydroxymuconate isomerase, SDS-PAGE
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme from Escherichia coli strain C by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, ultrafiltration, ammoniums ulfate fractionation, and hydrophobic interaction chromatography, followed by gel filtration
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxymuconate
stereospecific ketonization
719634
Pseudomonas putida
2-oxo-3-(E)-hexenedioate
-
-
-
?
2-hydroxymuconate
stereospecific ketonization, a reaction of EC 5.3.2.6, is also catalyzed by 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10
719634
Escherichia coli
2-oxo-3-(E)-hexenedioate
-
-
-
?
2-hydroxymuconate
stereospecific ketonization
719634
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
2-oxo-3-(E)-hexenedioate
-
-
-
?
2-hydroxymuconate
stereospecific ketonization, a reaction of EC 5.3.2.6, is also catalyzed by 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10
719634
Escherichia coli C
2-oxo-3-(E)-hexenedioate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 14000, 5-(carboxymethyl)-2-hydroxymuconate isomerase, SDS-PAGE
Escherichia coli
?
x * 3600, 4-oxalocrotonate tautomerase, SDS-PAGE
Pseudomonas putida
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
30
-
assay at
Pseudomonas putida
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Escherichia coli
7.3
-
assay at
Pseudomonas putida
General Information
General Information
Commentary
Organism
evolution
mechanism and the evolution of 4-oxalocrotonate tautomerase, EC 5.3.2.6, and 5-(carboxymethyl)-2-hydroxymuconate isomerase and their respective pathways, overview
Escherichia coli
evolution
mechanism and the evolution of 4-oxalocrotonate tautomerase, and 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10, and their respective pathways, overview
Pseudomonas putida
metabolism
in the homoprotocatechuate pathway elaborated by Escherichia coli C ketonization of 5-(carboxymethyl)-2-hydroxymuconate by 5-(carboxymethyl)-2-hydroxymuconate isomerase generates the alpha,beta-unsaturated ketone, which undergoes decarboxylation and further processing to intermediates in the Krebs cycle
Escherichia coli
metabolism
in the catechol meta-fission pathway elaborated by Pseudomonas putida mt-2 ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase generates the alpha,beta-unsaturated ketone 2-oxo-3-(E)-hexenedioate, which undergoes decarboxylation and further processing to intermediates in the Krebs cycle
Pseudomonas putida
General Information (protein specific)
General Information
Commentary
Organism
evolution
mechanism and the evolution of 4-oxalocrotonate tautomerase, EC 5.3.2.6, and 5-(carboxymethyl)-2-hydroxymuconate isomerase and their respective pathways, overview
Escherichia coli
evolution
mechanism and the evolution of 4-oxalocrotonate tautomerase, and 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10, and their respective pathways, overview
Pseudomonas putida
metabolism
in the homoprotocatechuate pathway elaborated by Escherichia coli C ketonization of 5-(carboxymethyl)-2-hydroxymuconate by 5-(carboxymethyl)-2-hydroxymuconate isomerase generates the alpha,beta-unsaturated ketone, which undergoes decarboxylation and further processing to intermediates in the Krebs cycle
Escherichia coli
metabolism
in the catechol meta-fission pathway elaborated by Pseudomonas putida mt-2 ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase generates the alpha,beta-unsaturated ketone 2-oxo-3-(E)-hexenedioate, which undergoes decarboxylation and further processing to intermediates in the Krebs cycle
Pseudomonas putida
Other publictions for EC 5.3.2.6
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)
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57
1012-1021
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18
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3
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4
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2
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3
1
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18
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3
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2
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3
1
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749336
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The S. aureus 4-oxalocrotonat ...
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Sci. Rep.
7
1745
2017
-
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1
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3
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2
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5
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2
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748503
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Importance of N-terminal prol ...
Pseudomonas putida
J. Serb. Chem. Soc.
81
871-881
2016
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1
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1
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1
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4
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748742
van der Meer
Using mutability landscapes o ...
Pseudomonas putida
Nat. Commun.
7
10911
2016
-
-
1
1
6
-
-
-
-
-
-
2
-
1
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1
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-
10
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1
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1
6
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2
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1
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10
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747290
Djokic
Immobilization of Escherichia ...
Pseudomonas putida
Bioprocess Biosyst. Eng.
38
2389-2395
2015
-
-
1
-
-
-
-
-
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1
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3
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2
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2
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747537
Poddar
Evidence for the formation of ...
Pseudomonas putida
ChemBioChem
16
738-741
2015
-
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-
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1
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1
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1
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2
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746910
Huddleston
Identification and characteri ...
Pseudomonas putida
Arch. Biochem. Biophys.
564
189-196
2014
-
-
-
-
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-
1
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1
-
1
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2
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747782
Baas
Demethionylation of Pro-1 var ...
Pseudomonas putida
FEBS Open Bio
4
651-658
2014
-
-
1
-
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1
-
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1
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2
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1
1
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1
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1
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1
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1
1
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1
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1
1
749284
Radivojevic
-
Synthesis of gamma-nitroaldeh ...
Pseudomonas putida
RSC Adv.
4
60502-60510
2014
-
-
1
-
-
-
-
-
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1
-
1
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7
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1
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1
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7
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-
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726816
Terrell
Structural and kinetic charact ...
Methylibium petroleiphilum
Arch. Biochem. Biophys.
537
113-124
2013
-
-
1
1
-
-
-
4
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1
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2
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1
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3
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4
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1
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1
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4
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1
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1
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3
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4
-
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4
4
727187
Narancic
Highly efficient Michael-type ...
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142
462-468
2013
-
-
1
-
-
-
-
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-
1
1
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2
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1
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5
1
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1
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1
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1
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5
1
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727314
Miao
Promiscuous catalysis of asymm ...
Bacillus subtilis
ChemBioChem
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191-194
2013
-
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1
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1
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8
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8
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727327
Geertsema
Biocatalytic Michael-type addi ...
Escherichia coli
Chemistry
19
14407-14410
2013
-
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1
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1
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8
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8
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720309
Wu
Catalytic mechanism of 4-oxalo ...
Pseudomonas putida
J. Phys. Chem. B
116
6889-6897
2012
-
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1
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3
3
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726964
Burks
Kinetic, crystallographic, and ...
Pseudomonas putida
Biochemistry
50
7600-7611
2011
-
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1
1
4
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1
6
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1
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1
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4
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8
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6
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6
6
718874
Burks
Kinetic and structural charact ...
Chloroflexus aurantiacus, Chloroflexus aurantiacus J-10-fl
Biochemistry
49
5016-5027
2010
-
-
1
1
5
-
-
12
-
-
3
2
-
5
-
-
1
-
-
-
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8
2
1
-
1
12
1
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1
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1
5
-
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12
-
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3
2
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1
-
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8
2
1
-
1
12
1
-
-
-
-
3
3
-
12
12
721792
Almrud
Kinetic and structural charact ...
Archaeoglobus fulgidus, Helicobacter pylori
Bioorg. Chem.
38
252-259
2010
-
-
2
2
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8
-
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4
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2
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8
2
2
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7
2
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2
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2
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8
-
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2
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8
2
2
-
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7
2
-
-
-
-
-
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-
8
8
704310
Kasai
Uncovering the protocatechuate ...
Paenibacillus sp., Paenibacillus sp. JJ-1b
J. Bacteriol.
191
6758-6768
2009
-
-
1
-
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2
-
2
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1
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1
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1
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1
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1
-
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2
-
1
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1
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1
1
-
-
-
718847
Wang
Kinetic and stereochemical ana ...
Bacillus subtilis, Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
Biochemistry
46
11919-11929
2007
-
-
1
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2
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4
-
21
-
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1
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10
2
2
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2
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1
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2
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4
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1
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10
2
2
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2
-
-
-
-
1
1
-
-
-
718844
Poelarends
Evolution of enzymatic activit ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
Biochemistry
45
7700-7708
2006
-
-
1
-
3
-
-
5
-
-
-
4
-
21
-
-
1
-
-
-
-
-
4
1
1
-
-
4
1
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
5
-
-
-
4
-
-
-
1
-
-
-
-
4
1
1
-
-
4
1
-
-
-
-
1
1
-
4
4
718840
Azurmendi
Half-of-the-sites binding of r ...
Pseudomonas putida
Biochemistry
44
7725-7737
2005
-
-
-
-
1
-
4
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
4
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
718830
Harris
Kinetic, stereochemical, and s ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
Biochemistry
38
12343-12357
1999
-
-
1
-
5
-
1
6
-
-
-
2
-
19
-
-
1
1
-
-
-
-
6
1
1
-
-
7
1
-
-
-
-
-
-
-
-
1
-
-
5
-
-
1
-
6
-
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
7
1
-
-
-
-
2
2
-
7
7
718825
Subramanya
Enzymatic ketonization of 2-hy ...
Pseudomonas sp., Pseudomonas sp. CF 600
Biochemistry
35
792-802
1996
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
718826
Stivers
Catalytic role of the amino-te ...
Pseudomonas sp., Pseudomonas sp. CF 600
Biochemistry
35
803-813
1996
-
-
-
-
-
-
1
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
719636
Fitzgerald
-
Total chemical synthesis and c ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Am. Chem. Soc.
117
11075-11080
1995
-
-
-
-
-
-
-
2
-
-
-
2
-
19
-
-
-
-
-
-
-
-
4
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
-
-
4
1
1
-
-
2
1
-
-
-
-
1
1
-
2
2
719634
Whitman
-
Stereospecific ketonization of ...
Escherichia coli, Escherichia coli C, Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Am. Chem. Soc.
114
10104-10110
1992
-
-
-
-
-
-
-
-
-
-
1
-
-
27
-
-
1
-
-
-
-
-
4
2
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
4
2
2
-
-
-
2
-
-
-
-
4
4
-
-
-
719633
Whitman
-
Chemical and enzymatic ketoniz ...
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
J. Am. Chem. Soc.
113
3154-3162
1991
-
-
1
-
-
-
-
3
-
-
-
2
-
19
-
-
1
-
-
-
-
-
10
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
2
-
-
-
1
-
-
-
-
10
-
1
-
-
2
1
-
-
-
-
2
2
-
2
2