5.3.2.6: 2-hydroxymuconate tautomerase
This is an abbreviated version!
For detailed information about 2-hydroxymuconate tautomerase, go to the full flat file.
Word Map on EC 5.3.2.6
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5.3.2.6
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tautomerization
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michael-type
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trans-3-chloroacrylic
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5-carboxymethyl-2-hydroxymuconate
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2-oxo-3-pentynoate
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stivers
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dienolic
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heterohexamer
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2-hydroxy-2,4-pentadienoate
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3-bromopyruvate
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beta-alpha-beta
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whitman
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proline-based
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3-chloroacrylic
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cis-caad
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meta-fission
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cis-3-chloroacrylic
- 5.3.2.6
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tautomerization
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michael-type
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trans-3-chloroacrylic
- 5-carboxymethyl-2-hydroxymuconate
- 2-oxo-3-pentynoate
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stivers
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dienolic
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heterohexamer
- 2-hydroxy-2,4-pentadienoate
- 3-bromopyruvate
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beta-alpha-beta
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whitman
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proline-based
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3-chloroacrylic
- cis-caad
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meta-fission
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cis-3-chloroacrylic
Reaction
Synonyms
4-OT, 4-oxalocrotonate tautomerase, 4-oxalocrotonate tautomerase I, 4-oxalocrotonate tautomerase II, 4OT, AfDmpI, D-4-oxalocrotonate tautomerase, HpDmpI, L-4-oxalocrotonate tautomerase, OCA, PRAC, SAR1376, TomN, xylH, YwhB
ECTree
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General Information
General Information on EC 5.3.2.6 - 2-hydroxymuconate tautomerase
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evolution
malfunction
metabolism
physiological function
additional information
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4-oxalocrotonate tautomerase is a member of the tautomerase superfamily
evolution
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mechanism and the evolution of 4-oxalocrotonate tautomerase, and 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10, and their respective pathways, overview
evolution
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mechanism and the evolution of 4-oxalocrotonate tautomerase, EC 5.3.2.6, and 5-(carboxymethyl)-2-hydroxymuconate isomerase and their respective pathways, overview
evolution
the enzyme is a member of the tautomerase superfamily
evolution
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the enzyme is a member of the tautomerase superfamily
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evolution
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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mechanism and the evolution of 4-oxalocrotonate tautomerase, and 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10, and their respective pathways, overview
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evolution
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mechanism and the evolution of 4-oxalocrotonate tautomerase, EC 5.3.2.6, and 5-(carboxymethyl)-2-hydroxymuconate isomerase and their respective pathways, overview
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covalent modification of Pro-1 by 3-bromopropiolate inactivates YwhB, implicating Pro-1 as a critical catalytic residue in the conversion of phenylenolpyruvate to phenylpyruvate
malfunction
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introduction of polar residues into the active site produces significant decreases in kcat and Km
malfunction
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modification by 3-bromopyruvate of three active sites per hexamer abolishes essentially all activity of the hexamer, spectrocopic and sequence analysis of labeled peptides, overview
malfunction
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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introduction of polar residues into the active site produces significant decreases in kcat and Km
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malfunction
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modification by 3-bromopyruvate of three active sites per hexamer abolishes essentially all activity of the hexamer, spectrocopic and sequence analysis of labeled peptides, overview
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4-oxalocrotonate tautomerase is an essential enzyme in the degradative metabolism pathway occurring in the Krebs cycle
metabolism
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4-oxalocrotonate tautomerase is part of a set of inducible enzymes that converts aromatic hydrocarbons to intermediates in the Krebs cycle
metabolism
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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
metabolism
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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
metabolism
the enzyme is involved in the degradation of 4-hydroxybenzoate via the protocatechuate 2,3-cleavage pathway, overview
metabolism
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the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle
metabolism
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle
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metabolism
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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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
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metabolism
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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4-oxalocrotonate tautomerase is part of a set of inducible enzymes that converts aromatic hydrocarbons to intermediates in the Krebs cycle
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metabolism
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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
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4-OT catalyzes the ketonization process of 2-oxo-4-hexenedioate to its conjugated isomer, 2-oxo-3-hexadienedioate, through the dienol intermediate 2-hydroxymuconate. This proton transfer process is an essential part of degradative metabolism pathway to convert various aromatic hydrocarbons into their corresponding intermediates in the Krebs cycle
physiological function
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4-oxalocrotonate tautomerase is an extremely efficient catalyst apparently processing either isomer near the diffusion control limit of a small molecule and an enzyme
physiological function
4-oxalocrotonate tautomerase isozymes play prominent roles in the bacterial utilization of aromatic hydrocarbons as sole carbon sources
physiological function
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4-oxalocrotonate tautomerase isozymes play prominent roles in the bacterial utilization of aromatic hydrocarbons as sole carbon sources
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physiological function
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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4-oxalocrotonate tautomerase is an extremely efficient catalyst apparently processing either isomer near the diffusion control limit of a small molecule and an enzyme
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immediate nonenzymatic conversion of 2-oxo-3-hexenedioate to 2-hydroxy-3-trans-hexenedioate with NaBH4. Rate constants for the nonenzymatic phosphate-catalyzed ketonization of 2-hydroxymuconate, overview
additional information
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structure-function relationship and kinetic analysis, detailed overview
additional information
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structure-function relationship, spectroscopic NMR analysis, detailed overview. Three arginine residues, Arg11, Arg39, and Arg61, are localized in the active site of 4-oxalocrotonate tautomerase. Importance of Arg11 in properly orienting the dicarboxylate substrate by interacting with the charged 6-carboxylate group. Arg39 interacts with the 1-carboxylate and the 2-keto group of the substrate to promote carbonyl polarization and catalysis, while Pro-1 transfers protons from C-3 to C-5. Arg61 does not play a significant role in either substrate binding or catalysis
additional information
the fully functional enzyme requires both subunits, active site structure and function of hh4-OT, overview. Three type II sites are formed at the other end of the heterodimeric unit interface around betaPro-1. As with the type I sites, two of the type II active site sides are composed of loops, but these loops are contributed from different subunits, that is, the alphaA'beta2' loop in the beta-subunit and the beta1alphaA loop in the alpha-subunit. The third side of the type II active site is composed of the intramonomeric alpha-subunit beta2-beta3 loop instead of a 310 helix
additional information
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the fully functional enzyme requires both subunits, active site structure and function of hh4-OT, overview. Three type II sites are formed at the other end of the heterodimeric unit interface around betaPro-1. As with the type I sites, two of the type II active site sides are composed of loops, but these loops are contributed from different subunits, that is, the alphaA'beta2' loop in the beta-subunit and the beta1alphaA loop in the alpha-subunit. The third side of the type II active site is composed of the intramonomeric alpha-subunit beta2-beta3 loop instead of a 310 helix
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additional information
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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structure-function relationship, spectroscopic NMR analysis, detailed overview. Three arginine residues, Arg11, Arg39, and Arg61, are localized in the active site of 4-oxalocrotonate tautomerase. Importance of Arg11 in properly orienting the dicarboxylate substrate by interacting with the charged 6-carboxylate group. Arg39 interacts with the 1-carboxylate and the 2-keto group of the substrate to promote carbonyl polarization and catalysis, while Pro-1 transfers protons from C-3 to C-5. Arg61 does not play a significant role in either substrate binding or catalysis
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additional information
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
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immediate nonenzymatic conversion of 2-oxo-3-hexenedioate to 2-hydroxy-3-trans-hexenedioate with NaBH4. Rate constants for the nonenzymatic phosphate-catalyzed ketonization of 2-hydroxymuconate, overview
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