Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
=
(3E)-2-oxohex-3-enedioate

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

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.2 Interconverting keto- and enol-groups
                5.3.2.6 2-hydroxymuconate tautomerase

Engineering

Engineering on EC 5.3.2.6 - 2-hydroxymuconate tautomerase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P1A
-
site-directed mutagenesis, inactive mutant
R11A
-
site-directed mutagenesis, inactive mutant
alphaR12A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT
alphaR40A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT
betaP1A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT
betaR11A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type hh4-OT
betaR39A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT
alphaR12A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT
-
alphaR40A
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT
-
betaP1A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT
-
betaR11A
-
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type hh4-OT
-
betaR39A
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT
-
A33D
the mutant shows highest enantioselectivity for the Michael-type addition of acetaldehyde to trans-beta nitrostyrene producing 4-nitro-3-phenylbutanal, compared to the wild type enzyme
A33E
the mutation significantly (4fold) improves the activity of the enzyme for the Michael-type addition of acetaldehyde to trans-beta nitrostyrene, compared to the wild type enzyme
alphaI52E
-
site-directed mutagenesis, active site mutant,the mutant shows improved trans-3-chloroacrylic acid dehalogenase activity with a 36fold increase in kcat/Km, largely due to a 110fold decrease in Km, and diminished 4-oxalocrotonate tautomerase activity. The negatively charged group may hinder the formation of the enolate intermediate and may contribute to a decrease in kcat
alphaL8R
-
site-directed mutagenesis, active site mutant, the mutant shows improved trans-3-chloroacrylic acid dehalogenase activity with a 50fold increase in kcat/Km, primarily from an 8.8fold increase in kcat, and diminished 4-oxalocrotonate tautomerase activity with a 5fold decrease in kcat/Km. The increased CaaD activity of L8R-4-OT does not substantially diminish the original 4-OT activity
alphaL8R/I52E
-
site-directed mutagenesis, active site mutant, the mutant shows improved trans-3-chloroacrylic acid dehalogenase activity with a 32fold increase in kcat/Km, largely due to a 23fold decrease in Km, and diminished 4-oxalocrotonate tautomerase activity with a 1700fold decrease in kcat/Km
H6M
the mutant has about 3fold increased specific activity compared with that of wild type enzyme
H6M/A33E/F50V
the mutation strongly enhances the activity for the Michael-type addition of butanal to trans-beta nitrostyrene, compared to the wild type enzyme
M45Y/F50A
the mutant enzyme displays low Michael-type addition activity compared to the wild type enzyme
P1A
-
the mutation results in 430fold decreases in kcat/Km compared to the wild type enzyme
R11A/R39A
-
site-directed mutagenesis, inactive mutant
R39E
the mutant shows highest enantioselectivity for the Michael-type addition of butanal to trans-beta nitrostyrene, producing 2-ethyl-4-nitro-3-phenylbutanal, compared to the wild type enzyme
alphaI52E
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, active site mutant,the mutant shows improved trans-3-chloroacrylic acid dehalogenase activity with a 36fold increase in kcat/Km, largely due to a 110fold decrease in Km, and diminished 4-oxalocrotonate tautomerase activity. The negatively charged group may hinder the formation of the enolate intermediate and may contribute to a decrease in kcat
-
alphaL8R
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, active site mutant, the mutant shows improved trans-3-chloroacrylic acid dehalogenase activity with a 50fold increase in kcat/Km, primarily from an 8.8fold increase in kcat, and diminished 4-oxalocrotonate tautomerase activity with a 5fold decrease in kcat/Km. The increased CaaD activity of L8R-4-OT does not substantially diminish the original 4-OT activity
-
alphaL8R/I52E
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, active site mutant, the mutant shows improved trans-3-chloroacrylic acid dehalogenase activity with a 32fold increase in kcat/Km, largely due to a 23fold decrease in Km, and diminished 4-oxalocrotonate tautomerase activity with a 1700fold decrease in kcat/Km
-
R11A
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, no kinetic effects of the R11A mutation, the stereoselectivity of the R11A-catalyzed protonation at C-5 of the dicarboxylate substrate decreases, while the stereoselectivity of protonation at C-3 of the monocarboxylate substrate increases in comparison with wild-type 4-OT
-
R11A/R39A
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, inactive mutant
-
R39A
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, with 2-hydroxymuconate the R39A mutant shows decreased kcat by 125fold and increased Km by 1.5fold
-
R39Q
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, with 2-hydroxymuconate the R39Q mutant shows decreased kcat by 389fold and increased Km by 2.6fold, only the tight binding sites function catalytically in the R39Q mutant, structural changes in the R39Q mutant were mainly in the beta-hairpin from residues 50 to 57 which covers the active site
-
R61A
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
site-directed mutagenesis, Arg61 mutation does not affect either substrate binding or catalysis
-
R35A
the mutation disrupts catalysis and impairs protein multimerisation
R35Q
the mutation disrupts catalysis and impairs protein multimerisation
R35A
-
the mutation disrupts catalysis and impairs protein multimerisation
-
R35Q
-
the mutation disrupts catalysis and impairs protein multimerisation
-