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(1Z)-1-(nitromethylidene)-3a,4,5,6,7,7a-hexahydro-1H-indene + acetaldehyde
[1-(nitromethyl)-1H-inden-1-yl]acetaldehyde
-
-
-
-
?
(1Z)-4-methyl-1-nitropent-1-ene + acetaldehyde
5-methyl-3-(nitromethyl)hexanal
-
-
-
-
?
(2E)-2-hydroxy-3-phenylprop-2-enoate
2-oxo-3-phenylpropanoate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(2E)-5-oxohex-2-enedioate
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(2E)-5-oxohex-2-enedioic acid
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
(3E)-6-oxohept-3-enedioate
2-hydroxy-2,4-heptadiene-1,7-dioate
-
-
-
-
?
(E)-1-nitro-2-(2-thienyl)ethene + isobutanal
2,2-dimethyl-4-nitro-3-(thiophen-2-yl)butanal
-
-
-
-
?
(E)-2-(furan-2-yl)nitroethene + isobutanal
3-(furan-2-yl)-2,2-dimethyl-4-nitrobutanal
-
-
-
-
?
(E)-2-(thiophen-2-yl)nitroethene + isobutanal
2,2-dimethyl-4-nitro-3-(thiophen-2-yl)butanal
-
-
-
-
?
1-chloro-4-[(Z)-2-nitroethenyl]benzene + acetaldehyde
3-(4-chlorophenyl)-4-nitrobutanal
-
-
-
-
?
1-fluoro-4-[(Z)-2-nitroethenyl]benzene + acetaldehyde
3-(4-fluorophenyl)-4-nitrobutanal
-
-
-
-
?
2-(cyclopentyloxy)-1-methoxy-4-[(Z)-2-nitroethenyl]benzene + acetaldehyde
3-[3-(cyclopentyloxy)-4-methoxyphenyl]-4-nitrobutanal
-
-
-
-
?
2-chloro-beta-nitrostyrene + acetaldehyde
3-(2-chlorophenyl)-4-nitrobutanal
-
-
51% yield
-
?
2-hydroxy-2,4-heptadiene-1,7-dioate
(3E)-2-oxohept-3-enedioate
-
-
-
-
?
2-hydroxy-2,4-hexadienedioate
2-oxo-3,4-hexenedioate
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
2-hydroxy-2,4-pentadienoate
(3E)-2-oxopent-3-enoate
-
-
-
-
?
2-hydroxy-2,4-pentadienoate
2-oxo-4-pentenoate
2-hydroxy-2,4-pentadienoate
2-oxopent-3-enoic acid
-
-
-
-
?
2-hydroxy-4-trans-hexenedioate
?
2-hydroxymuconate
2-oxo-3-(E)-hexenedioate
2-hydroxymuconate
2-oxo-3-hexenedioate
2-hydroxymuconate
4-oxalocrotonate
-
-
-
?
2-methoxy-5-[(Z)-2-nitroethenyl]phenol + acetaldehyde
3-(3-hydroxy-4-methoxyphenyl)-4-nitrobutanal
-
-
-
-
?
2-oxo-3-hexenedioate
2-oxo-3-trans-hexenedioate
2-oxo-4(E)-hexenedioate
2-oxo-3(E)-hexenedioate
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
2-oxopent-4-enoate
2-hydroxy-2,4-pentadienoate
-
-
-
-
?
3,4-(methylenedioxy)-beta-nitrostyrene + isobutanal
(3E)-3-(2H-1,3-benzodioxol-5-yl)-2,2-dimethyl-4-nitrobut-3-enal
-
-
-
-
?
4-chloro-beta-nitrostyrene + acetaldehyde
3-(4-chlorophenyl)-4-nitrobutanal
-
-
38% yield
-
?
4-fluoro-beta-nitrostyrene + acetaldehyde
3-(4-fluorophenyl)-4-nitrobutanal
-
-
31% yield
-
?
4-vinyl-2,3-dihydropyrrole-2-carboxylic acid
4-ethylidene-3,4-dihydropyrrole-2-carboxylic acid
-
-
-
-
r
5-(methyl)-2-hydroxymuconate
5-(methyl)-2-oxo-3-hexenedioate
-
-
-
?
acetaldehyde + (1Z)-4-methyl-1-nitropent-1-ene
6-methyl-4-(nitromethyl)heptan-2-one
-
-
-
r
acetaldehyde + 1-chloro-4-[(E)-2-nitroethenyl]benzene
4-(4-chlorophenyl)-5-nitropentan-2-one
-
-
-
r
acetaldehyde + 1-fluoro-4-[(E)-2-nitroethenyl]benzene
4-(4-fluorophenyl)-5-nitropentan-2-one
-
-
-
r
acetaldehyde + 2-(cyclopentyloxy)-1-methoxy-4-[(E)-2-nitroethenyl]benzene
4-[3-(cyclopentyloxy)-4-methoxyphenyl]-5-nitropentan-2-one
-
-
-
r
acetaldehyde + 2-methoxy-5-[(E)-2-nitroethenyl]phenol
4-(3-hydroxy-4-methoxyphenyl)-5-nitropentan-2-one
-
-
-
r
acetaldehyde + 4-[(E)-2-nitroethenyl]phenol
4-(4-hydroxyphenyl)-5-nitropentan-2-one
-
-
-
r
acetaldehyde + benzaldehyde
cinnamaldehyde
-
-
-
r
acetaldehyde + [(E)-2-nitroethenyl]benzene
5-nitro-4-phenylpentan-2-one
-
-
-
r
acetaldehyde + [(Z)-2-nitroethenyl]benzene
(3S)-4-nitro-3-phenylbutanal
-
-
-
-
?
beta-nitrostyrene + acetaldehyde
4-nitro-3-phenyl-butanal
-
-
60% yield
-
?
beta-nitrostyrene + acetaldehyde
4-nitro-3-phenylbutanal
-
-
-
-
r
beta-nitrostyrene + isobutanal
2,2-dimethyl-4-nitro-3-phenylbutanal
-
-
-
-
?
butanal + [(E)-2-nitroethenyl]benzene
3-ethyl-5-nitro-4-phenylpentan-2-one
-
-
-
r
butanal + [(Z)-2-nitroethenyl]benzene
(2R,3S)-2-ethyl-4-nitro-3-phenylbutanal
-
-
-
-
?
heptanal + [(Z)-2-nitroethenyl]benzene
(2R)-2-[(1S)-2-nitro-1-phenylethyl]heptanal
-
-
-
-
?
hexanal + [(Z)-2-nitroethenyl]benzene
(2R)-2-[(1S)-2-nitro-1-phenylethyl]hexanal
-
-
-
-
?
isobutanal + beta-nitrostyrene
2,2-dimethyl-4-nitro-3-phenylbutanal + 4-nitro-3-phenylbutanal
-
-
-
-
?
octanal + [(Z)-2-nitroethenyl]benzene
(2R)-2-[(1S)-2-nitro-1-phenylethyl]octanal
-
-
-
-
?
pentanal + [(Z)-2-nitroethenyl]benzene
(2R)-2-[(1S)-2-nitro-1-phenylethyl]pentanal
-
-
-
-
?
phenylenolpyruvate
phenylpyruvate
propanal + [(Z)-2-nitroethenyl]benzene
(2R,3S)-2-methyl-4-nitro-3-phenylbutanal
-
-
-
-
?
trans-p-chloro-beta-nitrostyrene + isobutanal
3-(4-chlorophenyl)-2,2-dimethyl-4-nitrobutanal
-
-
-
-
?
[(Z)-2-nitroethenyl]benzene + acetaldehyde
4-nitro-3-phenylbutanal
-
-
-
-
?
additional information
?
-
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(2E)-5-oxohex-2-enedioate
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(2E)-5-oxohex-2-enedioate
-
1,3- and 1,5-keto-enol tautomerization reactions are observed for 2-hydroxy-2,4-hexadienedioate. YwhB converts it to the 3S isomer of 2-oxo-4-hexenedioate in a highly stereoselective manner
main product
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3,4-hexenedioate
-
4-OT with 2-hydroxy-2,4-hexadienedioate in D2O results in a racemic mixture of 2-oxo-[3-2H]-4-hexenedioate, suggesting that 4-OT may not catalyze a 1,3-keto-enol tautomerization reaction using this dienol
-
-
?
2-hydroxy-2,4-hexadienedioate
2-oxo-3,4-hexenedioate
-
4-OT with 2-hydroxy-2,4-hexadienedioate in D2O results in a racemic mixture of 2-oxo-[3-2H]-4-hexenedioate, suggesting that 4-OT may not catalyze a 1,3-keto-enol tautomerization reaction using this dienol
-
-
?
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
i.e. 2-hydroxymuconate
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
i.e. 2-hydroxymuconate, the enzyme catalyzes the conversion of 2-hydroxy-2,4-hexadienedioate (or 2-hydroxymuconate) to 2-oxo-3-hexenedioate, where Pro-1 functions as a general base and shuttles a proton from the 2-hydroxyl group of the substrate to the C-5 position of the product. hh4-OT requires the amino-terminal proline and two arginines for the conversion of 2-hydroxymuconate to the product
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
i.e. 2-hydroxymuconate
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
i.e. 2-hydroxymuconate, the enzyme catalyzes the conversion of 2-hydroxy-2,4-hexadienedioate (or 2-hydroxymuconate) to 2-oxo-3-hexenedioate, where Pro-1 functions as a general base and shuttles a proton from the 2-hydroxyl group of the substrate to the C-5 position of the product. hh4-OT requires the amino-terminal proline and two arginines for the conversion of 2-hydroxymuconate to the product
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
-
-
-
-
?
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
-
-
-
-
?
2-hydroxy-2,4-pentadienoate
2-oxo-4-pentenoate
-
-
-
?
2-hydroxy-2,4-pentadienoate
2-oxo-4-pentenoate
-
-
-
-
?
2-hydroxy-4-trans-hexenedioate
?
-
-
-
-
?
2-hydroxy-4-trans-hexenedioate
?
-
-
-
-
?
2-hydroxymuconate
2-oxo-3-(E)-hexenedioate
-
stereospecific ketonization, a reaction of EC 5.3.2.6, is also catalyzed by 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10
-
-
?
2-hydroxymuconate
2-oxo-3-(E)-hexenedioate
-
stereospecific ketonization, a reaction of EC 5.3.2.6, is also catalyzed by 5-(carboxymethyl)-2-hydroxymuconate isomerase, EC 5.3.3.10
-
-
?
2-hydroxymuconate
2-oxo-3-(E)-hexenedioate
-
stereospecific ketonization
-
-
?
2-hydroxymuconate
2-oxo-3-(E)-hexenedioate
-
stereospecific ketonization
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
-
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
-
-
-
-
r
2-hydroxymuconate
2-oxo-3-hexenedioate
-
ketonization
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
-
ketonization
-
-
r
2-hydroxymuconate
2-oxo-3-hexenedioate
-
the conjugated enol, 2-hydroxymuconate is an unusually stable dienol that is reportedly generated in the course of bacterial catabolism of catechol by the enzymes of the meta-fission pathway
the dienol ketonizes chemically in aqueous solution and enzymatically by the action of 4-oxalocrotonate tautomerase to either the beta,gamma-unsaturated ketone or its alpha,beta-conjugated isomer 2-oxo-3-trans-hexenedioate
-
r
2-hydroxymuconate
2-oxo-3-hexenedioate
-
ketonization
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
-
ketonization
-
-
r
2-hydroxymuconate
2-oxo-3-hexenedioate
-
the conjugated enol, 2-hydroxymuconate is an unusually stable dienol that is reportedly generated in the course of bacterial catabolism of catechol by the enzymes of the meta-fission pathway
the dienol ketonizes chemically in aqueous solution and enzymatically by the action of 4-oxalocrotonate tautomerase to either the beta,gamma-unsaturated ketone or its alpha,beta-conjugated isomer 2-oxo-3-trans-hexenedioate
-
r
2-oxo-3-hexenedioate
2-oxo-3-trans-hexenedioate
-
-
-
-
?
2-oxo-3-hexenedioate
2-oxo-3-trans-hexenedioate
-
-
-
-
?
2-oxo-4(E)-hexenedioate
2-oxo-3(E)-hexenedioate
-
1,3-allylic isomerization
-
-
?
2-oxo-4(E)-hexenedioate
2-oxo-3(E)-hexenedioate
-
1,3-allylic isomerization
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
ketonization process via dienol intermediate 2-hydroxymuconate and with Pro1 as a general base, one-proton transfer mechanism
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via dienol intermediate 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via the intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
the enzyme converts the unconjugated enone to the conjugated enone via a dienolic intermediate 2-hydroxymuconate, Pro1 serves as the general base, and both Arg11 and Arg39 function in substrate binding and catalysis in an otherwise hydrophobic active site. Anticooperativity during catalysis
-
-
r
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via dienol intermediate 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via the intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
phenylenolpyruvate
phenylpyruvate
-
-
-
?
phenylenolpyruvate
phenylpyruvate
-
-
-
-
?
phenylenolpyruvate
phenylpyruvate
-
-
-
r
phenylenolpyruvate
phenylpyruvate
-
-
-
r
phenylenolpyruvate
phenylpyruvate
-
-
-
-
?
phenylenolpyruvate
phenylpyruvate
-
-
-
r
additional information
?
-
-
YwhB has a relatively non-specific 1,3- and 1,5-keto-enol tautomerase activity, converting 2-hydroxy-2,4-pentadienoate to 2-oxo-4-pentenoate, and phenylenolpyruvate to phenylpyruvate. But YwhB is a more efficient 1,3-keto-enol tautomerase than it is a 1,5-keto-enol tautomerase, and residues Pro-1 and Arg-11 are critical residues for these two activities
-
-
?
additional information
?
-
hh4-OT does not exhibit the low-level activity of another tautomerase superfamily member, the heterohexamer trans-3-chloroacrylic acid dehalogenase, no activity with trans-3-chloroacrylic acid
-
-
?
additional information
?
-
hh4-OT does not exhibit the low-level activity of another tautomerase superfamily member, the heterohexamer trans-3-chloroacrylic acid dehalogenase, no activity with trans-3-chloroacrylic acid
-
-
?
additional information
?
-
-
hh4-OT does not exhibit the low-level activity of another tautomerase superfamily member, the heterohexamer trans-3-chloroacrylic acid dehalogenase, no activity with trans-3-chloroacrylic acid
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
ketonization of two monoacid substrates, 2-hydroxy-2,4-pentadienoate and phenylenolpyruvate, produces a mixture of stereoisomers, 2-keto-3-[2H]-4-pentenoate and 3-[2H]-phenylpyruvate, where the (3R)-isomers predominate
-
-
?
additional information
?
-
-
the achiral substrate 2-hydroxymuconate is processed with equal efficiency by either the D- or the L-enzyme, stereochemical analysis of the D-4OT-catalyzed reaction, overviewn
-
-
?
additional information
?
-
-
no activity with (E)-2-cyclohexyl-1-nitroethene
-
-
?
additional information
?
-
-
the enzyme also has a low level trans-3-chloroacrylic acid dehalogenase activity
-
-
?
additional information
?
-
-
ketonization of two monoacid substrates, 2-hydroxy-2,4-pentadienoate and phenylenolpyruvate, produces a mixture of stereoisomers, 2-keto-3-[2H]-4-pentenoate and 3-[2H]-phenylpyruvate, where the (3R)-isomers predominate
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the achiral substrate 2-hydroxymuconate is processed with equal efficiency by either the D- or the L-enzyme, stereochemical analysis of the D-4OT-catalyzed reaction, overviewn
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
4-oxalocrotonate tautomerase catalyzes the isomerization of unsaturated 2-oxo acids, converting unconjugated ketones to the conjugated isomers via a dienolic intermediate
-
-
?
additional information
?
-
-
4-oxalocrotonate tautomerase catalyzes the isomerization of unsaturated 2-oxo acids, converting unconjugated ketones to the conjugated isomers via a dienolic intermediate
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
2-hydroxy-2,4-pentadienoate
2-oxopent-3-enoic acid
-
-
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
2-hydroxymuconate
4-oxalocrotonate
-
-
-
?
2-oxo-4(E)-hexenedioate
2-oxo-3(E)-hexenedioate
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
phenylenolpyruvate
phenylpyruvate
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
?
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
r
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
(3E)-2-oxohex-3-enedioate
-
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
i.e. 2-hydroxymuconate
-
-
r
2-hydroxy-2,4-hexadienedioate
2-oxo-3-hexenedioate
i.e. 2-hydroxymuconate
-
-
r
2-hydroxymuconate
2-oxo-3-hexenedioate
-
ketonization
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
-
the conjugated enol, 2-hydroxymuconate is an unusually stable dienol that is reportedly generated in the course of bacterial catabolism of catechol by the enzymes of the meta-fission pathway
the dienol ketonizes chemically in aqueous solution and enzymatically by the action of 4-oxalocrotonate tautomerase to either the beta,gamma-unsaturated ketone or its alpha,beta-conjugated isomer 2-oxo-3-trans-hexenedioate
-
r
2-hydroxymuconate
2-oxo-3-hexenedioate
-
ketonization
-
-
?
2-hydroxymuconate
2-oxo-3-hexenedioate
-
the conjugated enol, 2-hydroxymuconate is an unusually stable dienol that is reportedly generated in the course of bacterial catabolism of catechol by the enzymes of the meta-fission pathway
the dienol ketonizes chemically in aqueous solution and enzymatically by the action of 4-oxalocrotonate tautomerase to either the beta,gamma-unsaturated ketone or its alpha,beta-conjugated isomer 2-oxo-3-trans-hexenedioate
-
r
2-oxo-4(E)-hexenedioate
2-oxo-3(E)-hexenedioate
-
1,3-allylic isomerization
-
-
?
2-oxo-4(E)-hexenedioate
2-oxo-3(E)-hexenedioate
-
1,3-allylic isomerization
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
ketonization process via dienol intermediate 2-hydroxymuconate and with Pro1 as a general base, one-proton transfer mechanism
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via dienol intermediate 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via the intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
isomerization of unconjugated 2-oxo acids such as 2-oxo-4-hexenedioate, to its conjugated isomer via dienol intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via dienol intermediate 2-hydroxymuconate
-
-
?
2-oxo-4-hexenedioate
2-oxo-3-hexenedioate
-
via the intermediate 2-hydroxy-2,4-hexadienedioate, i.e. 2-hydroxymuconate
-
-
?
phenylenolpyruvate
phenylpyruvate
-
-
-
-
?
phenylenolpyruvate
phenylpyruvate
-
-
-
r
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0.334
(2E)-2-hydroxy-3-phenylprop-2-enoate
-
wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.05 - 0.17
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
0.017 - 1.6
2-hydroxy-2,4-hexadienedioate
0.09 - 1.11
2-hydroxy-2,4-pentadienoate
0.017 - 1.05
2-hydroxymuconate
0.189
2-oxo-3-hexenedioate
-
pH 7.3, 30°C
0.09 - 0.103
2-oxo-4(E)-hexenedioate
0.105 - 0.211
5-(methyl)-2-hydroxymuconate
0.063 - 0.23
phenylenolpyruvate
additional information
additional information
-
0.05
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
at pH 7.3 and 22°C
0.11
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate
0.11
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
pH 7.3, 23°C, conversion to compound 5
0.135
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
pH 7.3, 23°C, conversion to compound 5
0.17
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate
0.017
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A
0.069
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR11A
0.07
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant wild-type hh4-OT
0.135
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A
0.18
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, wild-type enzyme
0.29
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R11A/R39A
0.29
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R39A
0.345
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR40A
0.47
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R39Q
1.033
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A
1.6
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R11A
0.09
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C
0.19
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C
1.11
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C, mutant R11A
1.11
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C, wild-type enzyme
0.017
2-hydroxymuconate
-
mutant 4-OT L8R, pH 7.3, 23°C
0.027
2-hydroxymuconate
-
mutant 4-OT L8R/I52E, pH 7.3, 23°C
0.06
2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
0.062
2-hydroxymuconate
-
mutant 4-OT I52E, pH 7.3, 23°C
0.14
2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
0.145
2-hydroxymuconate
-
pH 7.3, 30°C
0.18
2-hydroxymuconate
-
wild-type 4-OT, pH 7.3, 23°C
0.18
2-hydroxymuconate
-
mutant enzyme P1A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.44
2-hydroxymuconate
-
mutant enzyme R39A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.512
2-hydroxymuconate
-
wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.78
2-hydroxymuconate
-
mutant enzyme R61A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
1.05
2-hydroxymuconate
-
mutant enzyme R11A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.09
2-oxo-4(E)-hexenedioate
-
D-4OT enantiomer, pH 7.3, 30°C
0.103
2-oxo-4(E)-hexenedioate
-
L-4OT enantiomer, pH 7.3, 30°C
0.105
5-(methyl)-2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
0.211
5-(methyl)-2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
0.063
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A
0.09
phenylenolpyruvate
pH 7.3, 23°C
0.121
phenylenolpyruvate
pH 7.3, 24°C, recombinant wild-type hh4-OT
0.143
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A
0.152
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR40A
0.159
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A
0.198
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR11A
0.23
phenylenolpyruvate
-
pH 7.3, 23°C
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
4-OT exhibits hyperbolic kinetics and shows anticooperativity during catalysis
-
additional information
additional information
-
kinetic modeling, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant 4-OTs for trans-3-chloroacrylic acid dehalogenase activity, pH 8.2, 23°C, overview
-
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16
(2E)-2-hydroxy-3-phenylprop-2-enoate
-
wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.05 - 1330
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
0.4 - 3500
2-hydroxy-2,4-hexadienedioate
0.1 - 2.5
2-hydroxy-2,4-pentadienoate
0.2 - 139000
2-hydroxymuconate
288000
2-oxo-3-hexenedioate
-
pH 7.3, 30°C
2890 - 2940
2-oxo-4(E)-hexenedioate
3.4 - 107
5-(methyl)-2-hydroxymuconate
0.2 - 44
phenylenolpyruvate
0.05
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
pH 7.3, 23°C, conversion to compound 5
0.2
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate
0.6
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate
0.6
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
pH 7.3, 23°C, conversion to compound 5
1330
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
at pH 7.3 and 22°C
0.4
2-hydroxy-2,4-hexadienedioate
-
below, pH 7.3, 23°C, mutant R11A/R39A
2 - 8
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R39A
3 - 6
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A
9
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R39Q
40
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R11A
43
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A
65
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR40A
733
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A
3000
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant wild-type hh4-OT
3500
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, wild-type enzyme
3500
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR11A
0.1
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C
0.4
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C, wild-type enzyme
1
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C, mutant R11A
2.5
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C
0.2
2-hydroxymuconate
-
mutant enzyme R39A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.3
2-hydroxymuconate
-
mutant 4-OT L8R/I52E, pH 7.3, 23°C
1.5
2-hydroxymuconate
-
mutant enzyme P1A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
14
2-hydroxymuconate
-
mutant enzyme R11A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
18.5
2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
32
2-hydroxymuconate
-
mutant 4-OT I52E, pH 7.3, 23°C
61
2-hydroxymuconate
-
mutant 4-OT L8R, pH 7.3, 23°C
360
2-hydroxymuconate
-
mutant enzyme R61A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
1850
2-hydroxymuconate
-
wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
3500
2-hydroxymuconate
-
wild-type 4-OT, pH 7.3, 23°C
4600
2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
139000
2-hydroxymuconate
-
pH 7.3, 30°C
2890
2-oxo-4(E)-hexenedioate
-
D-4OT enantiomer, pH 7.3, 30°C
2940
2-oxo-4(E)-hexenedioate
-
L-4OT enantiomer, pH 7.3, 30°C
3.4
5-(methyl)-2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
107
5-(methyl)-2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
0.2
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A
0.6
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A
2.4
phenylenolpyruvate
pH 7.3, 23°C
2.6
phenylenolpyruvate
-
pH 7.3, 23°C
11
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A
13
phenylenolpyruvate
pH 7.3, 24°C, recombinant wild-type hh4-OT
17
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR11A
44
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR40A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
48
(2E)-2-hydroxy-3-phenylprop-2-enoate
-
wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
0.45 - 26600
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
19 - 51000
2-hydroxy-2,4-hexadienedioate
0.36 - 13
2-hydroxy-2,4-pentadienoate
0.45 - 957000
2-hydroxymuconate
1520000
2-oxo-3-hexenedioate
-
pH 7.3, 30°C
29000 - 32000
2-oxo-4(E)-hexenedioate
16 - 1000
5-(methyl)-2-hydroxymuconate
3.2 - 290
phenylenolpyruvate
0.45
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
pH 7.3, 23°C, conversion to compound 5
1.2
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate
4.4
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
pH 7.3, 23°C, conversion to compound 5
5.4
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate
26600
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate
-
at pH 7.3 and 22°C
19
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R39Q
25
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R11A
42
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A
97
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R39A
190
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR40A
2100
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A
5400
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A
12000
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, mutant R11A/R39A
19000
2-hydroxy-2,4-hexadienedioate
-
pH 7.3, 23°C, wild-type enzyme
43000
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant wild-type hh4-OT
51000
2-hydroxy-2,4-hexadienedioate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR11A
0.36
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C, wild-type enzyme
0.9
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C, mutant R11A
1.1
2-hydroxy-2,4-pentadienoate
pH 7.3, 23°C
13
2-hydroxy-2,4-pentadienoate
-
pH 7.3, 23°C
0.45
2-hydroxymuconate
-
mutant enzyme R39A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
8.3
2-hydroxymuconate
-
mutant enzyme P1A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
11
2-hydroxymuconate
-
mutant 4-OT L8R/I52E, pH 7.3, 23°C
13
2-hydroxymuconate
-
mutant enzyme R11A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
310
2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
460
2-hydroxymuconate
-
mutant enzyme R61A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
520
2-hydroxymuconate
-
mutant 4-OT I52E, pH 7.3, 23°C
3600
2-hydroxymuconate
-
mutant 4-OT L8R, pH 7.3, 23°C
3600
2-hydroxymuconate
-
wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C
19000
2-hydroxymuconate
-
wild-type 4-OT, pH 7.3, 23°C
33000
2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
957000
2-hydroxymuconate
-
pH 7.3, 30°C
29000
2-oxo-4(E)-hexenedioate
-
L-4OT enantiomer, pH 7.3, 30°C
32000
2-oxo-4(E)-hexenedioate
-
D-4OT enantiomer, pH 7.3, 30°C
16
5-(methyl)-2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
1000
5-(methyl)-2-hydroxymuconate
isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C
3.2
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A
4.2
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A
11
phenylenolpyruvate
-
pH 7.3, 23°C
27
phenylenolpyruvate
pH 7.3, 23°C
70
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A
86
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant betaR11A
110
phenylenolpyruvate
pH 7.3, 24°C, recombinant wild-type hh4-OT
290
phenylenolpyruvate
pH 7.3, 24°C, recombinant hh4-OT mutant alphaR40A
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evolution
-
4-oxalocrotonate tautomerase is a member of the tautomerase superfamily
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
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
evolution
the enzyme is a member of the tautomerase superfamily
evolution
-
the enzyme is a member of the tautomerase superfamily
-
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
-
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
-
malfunction
-
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
-
introduction of polar residues into the active site produces significant decreases in kcat and Km
malfunction
-
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
-
introduction of polar residues into the active site produces significant decreases in kcat and Km
-
malfunction
-
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
-
metabolism
-
4-oxalocrotonate tautomerase is an essential enzyme in the degradative metabolism pathway occurring in the Krebs cycle
metabolism
-
4-oxalocrotonate tautomerase is part of a set of inducible enzymes that converts aromatic hydrocarbons to intermediates in the Krebs cycle
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
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
metabolism
the enzyme is involved in the degradation of 4-hydroxybenzoate via the protocatechuate 2,3-cleavage pathway, overview
metabolism
-
the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle
metabolism
-
the enzyme is part of a degradative pathway that converts various aromatic hydrocarbons to intermediates in the Krebs cycle
-
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
-
metabolism
-
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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physiological function
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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
-
4-oxalocrotonate tautomerase is an extremely efficient catalyst apparently processing either isomer near the diffusion control limit of a small molecule and an enzyme
-
additional information
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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
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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
-
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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?
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x * 14000, 5-(carboxymethyl)-2-hydroxymuconate isomerase, SDS-PAGE
?
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x * 14000, 5-(carboxymethyl)-2-hydroxymuconate isomerase, SDS-PAGE
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?
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x * 3600, 4-oxalocrotonate tautomerase, SDS-PAGE
?
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x * 6812, electrospray ionization mass spectrometry
?
x * 6812, electrospray ionization mass spectrometry
?
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x * 3600, 4-oxalocrotonate tautomerase, SDS-PAGE
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heterohexamer
3* 7730, alpha-subunit, + 3 * 7963, beta-subunit, mass spectrometry, 3 * 7732, alpha-subunit + 3 * 8096, beta-subunit, sequence calculation, functional heterohexamer OT, hh4-OT, composed of three alphabeta dimers, the fully functional enzyme requires both subunits
heterohexamer
-
3* 7730, alpha-subunit, + 3 * 7963, beta-subunit, mass spectrometry, 3 * 7732, alpha-subunit + 3 * 8096, beta-subunit, sequence calculation, functional heterohexamer OT, hh4-OT, composed of three alphabeta dimers, the fully functional enzyme requires both subunits
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hexamer
the betaalphabeta fold is conserved in the monomer
hexamer
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the betaalphabeta fold is conserved in the monomer
hexamer
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4-OT has an amino-terminal proline and a beta-alpha-beta fold, three structural models of 4-OT, overview
hexamer
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the noncovalent structures of each 4OT enantiomer are similar, the predominant form of the enzyme is a hexameric complex of identical subunits
hexamer
-
the noncovalent structures of each 4OT enantiomer are similar, the predominant form of the enzyme is a hexameric complex of identical subunits
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hexamer
subunits are arranged with 32 symmetry
hexamer
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subunits are arranged with 32 symmetry
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additional information
beta-subunit hh4-OT homology modeling derived from MODELER using the Pseudomonas sp. CF600 4OT isozyme, PDB entry 1OTF
additional information
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beta-subunit hh4-OT homology modeling derived from MODELER using the Pseudomonas sp. CF600 4OT isozyme, PDB entry 1OTF
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additional information
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structure determinatin and analysis by NMR of wild-type and mutant L8R 4-OTs, overview
additional information
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structure-function relationship, NMR analysis, overview
additional information
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structure-function relationship, NMR analysis, overview
-
additional information
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structure determinatin and analysis by NMR of wild-type and mutant L8R 4-OTs, overview
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additional information
monomeric and dimeric structure comparison of 4-oxalocrotonate tautomerase with monomeric 5-carboxymethyl-2-hydroxymuconate isomerase, overview. The region of greatest similarity between the two enzymes is a large pocket that is proposed to be the active site
additional information
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monomeric and dimeric structure comparison of 4-oxalocrotonate tautomerase with monomeric 5-carboxymethyl-2-hydroxymuconate isomerase, overview. The region of greatest similarity between the two enzymes is a large pocket that is proposed to be the active site
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P1A
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site-directed mutagenesis, inactive mutant
R11A
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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
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site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT
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alphaR40A
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT
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betaP1A
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site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT
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betaR11A
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site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type hh4-OT
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betaR39A
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT
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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
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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
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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
-
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
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alphaL8R
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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
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alphaL8R/I52E
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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
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R11A
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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
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R11A/R39A
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site-directed mutagenesis, inactive mutant
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R39A
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site-directed mutagenesis, with 2-hydroxymuconate the R39A mutant shows decreased kcat by 125fold and increased Km by 1.5fold
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R39Q
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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
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R61A
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site-directed mutagenesis, Arg61 mutation does not affect either substrate binding or catalysis
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R35A
the mutation disrupts catalysis and impairs protein multimerisation
R35Q
the mutation disrupts catalysis and impairs protein multimerisation
R35A
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the mutation disrupts catalysis and impairs protein multimerisation
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R35Q
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the mutation disrupts catalysis and impairs protein multimerisation
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R11A
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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
-
the mutation results in 280fold decreases in kcat/Km compared to the wild type enzyme
R39A
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site-directed mutagenesis, with 2-hydroxymuconate the R39A mutant shows decreased kcat by 125fold and increased Km by 1.5fold
R39A
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the mutation results in 8000fold decreases in kcat/Km compared to the wild type enzyme
R39Q
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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
R39Q
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titration with cis,cis-muconate shows negative cooperativity
R61A
-
site-directed mutagenesis, Arg61 mutation does not affect either substrate binding or catalysis
R61A
-
the mutation results in 8fold decreases in kcat/Km compared to the wild type enzyme
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Uncovering the protocatechuate 2,3-cleavage pathway genes
J. Bacteriol.
191
6758-6768
2009
Paenibacillus sp. (C4TP07)
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Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases
Biochemistry
35
792-802
1996
Pseudomonas sp. (P49172), Pseudomonas sp. CF 600 (P49172)
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Stivers, J.; Abeygunawardana, C.; Mildvan, A.; Hajipour, G.; Whitman, C.; Chen, L.
Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies
Biochemistry
35
803-813
1996
Pseudomonas sp., Pseudomonas sp. CF 600
brenda
Harris, T.K.; Czerwinski, R.M.; Johnson, W.H.; Legler, P.M.; Abeygunawardana, C.; Massiah, M.A.; Stivers, J.T.; Whitman, C.P.; Mildvan, A.S.
Kinetic, stereochemical, and structural effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase
Biochemistry
38
12343-12357
1999
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
brenda
Azurmendi, H.F.; Miller, S.G.; Whitman, C.P.; Mildvan, A.S.
Half-of-the-sites binding of reactive intermediates and their analogues to 4-oxalocrotonate tautomerase and induced structural asymmetry of the enzyme
Biochemistry
44
7725-7737
2005
Pseudomonas putida
brenda
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Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase
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45
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2006
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
brenda
Wang, S.; Johnson Jr., W.; Czerwinski, R.; Stamps, S.; Whitman, C.
Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: Mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions
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46
11919-11929
2007
Bacillus subtilis, Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
brenda
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Kinetic and structural characterization of a heterohexamer 4-oxalocrotonate tautomerase from Chloroflexus aurantiacus J-10-fl: implications for functional and structural diversity in the tautomerase superfamily
Biochemistry
49
5016-5027
2010
Chloroflexus aurantiacus (A9W9U6), Chloroflexus aurantiacus J-10-fl (A9W9U6), Chloroflexus aurantiacus J-10-fl
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Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol
J. Am. Chem. Soc.
113
3154-3162
1991
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
brenda
Whitman, C.; Hajipour, G.; Watson, R.; Johnson Jr., W.; Bembenek, M.; Stolowich, N.
Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase
J. Am. Chem. Soc.
114
10104-10110
1992
Escherichia coli, Escherichia coli C, Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
brenda
Fitzgerald, M.; Chernushevich, I.; Standing, K.; Kent, S.; Whitman, C.
Total chemical synthesis and catalytic properties of the enzyme enantiomers L- and D-4-oxalocrotonate tautomerase
J. Am. Chem. Soc.
117
11075-11080
1995
Pseudomonas putida, Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
brenda
Wu, P.; Cisneros, G.A.; Hu, H.; Chaudret, R.; Hu, X.; Yang, W.
Catalytic mechanism of 4-oxalocrotonate tautomerase: significances of protein-protein interactions on proton transfer pathways
J. Phys. Chem. B
116
6889-6897
2012
Pseudomonas putida
brenda
Almrud, J.J.; Dasgupta, R.; Czerwinski, R.M.; Kern, A.D.; Hackert, M.L.; Whitman, C.P.
Kinetic and structural characterization of DmpI from Helicobacter pylori and Archaeoglobus fulgidus, two 4-oxalocrotonate tautomerase family members
Bioorg. Chem.
38
252-259
2010
Helicobacter pylori, Archaeoglobus fulgidus (O29588), Archaeoglobus fulgidus
brenda
Terrell, C.R.; Burks, E.A.; Whitman, C.P.; Hoffman, D.W.
Structural and kinetic characterization of two 4-oxalocrotonate tautomerases in Methylibium petroleiphilum strain PM1
Arch. Biochem. Biophys.
537
113-124
2013
Methylibium petroleiphilum (A2SL37)
brenda
Burks, E.A.; Yan, W.; Johnson, W.H.; Li, W.; Schroeder, G.K.; Min, C.; Gerratana, B.; Zhang, Y.; Whitman, C.P.
Kinetic, crystallographic, and mechanistic characterization of TomN: elucidation of a function for a 4-oxalocrotonate tautomerase homologue in the tomaymycin biosynthetic pathway
Biochemistry
50
7600-7611
2011
Pseudomonas putida
brenda
Narancic, T.; Radivojevic, J.; Jovanovic, P.; Francuski, D.; Bigovic, M.; Maslak, V.; Savic, V.; Vasiljevic, B.; O'Connor, K.E.; Nikodinovic-Runic, J.
Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase
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142
462-468
2013
Pseudomonas putida
brenda
Miao, Y.; Geertsema, E.M.; Tepper, P.G.; Zandvoort, E.; Poelarends, G.J.
Promiscuous catalysis of asymmetric Michael-type additions of linear aldehydes to beta-nitrostyrene by the proline-based enzyme 4-oxalocrotonate tautomerase
ChemBioChem
14
191-194
2013
Bacillus subtilis
brenda
Geertsema, E.M.; Miao, Y.; Tepper, P.G.; de Haan, P.; Zandvoort, E.; Poelarends, G.J.
Biocatalytic Michael-type additions of acetaldehyde to nitroolefins with the proline-based enzyme 4-oxalocrotonate tautomerase yielding enantioenriched gamma-nitroaldehydes
Chemistry
19
14407-14410
2013
Escherichia coli
brenda
Huddleston, J.P.; Burks, E.A.; Whitman, C.P.
Identification and characterization of new family members in the tautomerase superfamily analysis and implications
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564
189-196
2014
Pseudomonas putida
brenda
Stack, T.M.M.; Li, W.; Johnson, W.H.; Zhang, Y.J.; Whitman, C.P.
Inactivation of 4-oxalocrotonate tautomerase by 5-halo-2-hydroxy-2,4-pentadienoates
Biochemistry
57
1012-1021
2018
Leptothrix cholodnii, Pseudomonas putida (Q01468), Leptothrix cholodnii SP-6
brenda
Djokic, L.; Spasic, J.; Jeremic, S.; Vasiljevic, B.; Prodanovic, O.; Prodanovic, R.; Nikodinovic-Runic, J.
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38
2389-2395
2015
Pseudomonas putida
brenda
Poddar, H.; Rahimi, M.; Geertsema, E.M.; Thunnissen, A.M.; Poelarends, G.J.
Evidence for the formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomerase
ChemBioChem
16
738-741
2015
Pseudomonas putida (Q01468)
brenda
Baas, B.J.; Zandvoort, E.; Wasiel, A.A.; Poelarends, G.J.
Demethionylation of Pro-1 variants of 4-oxalocrotonate tautomerase in Escherichia coli by co-expression with an engineered methionine aminopeptidase
FEBS Open Bio
4
651-658
2014
Pseudomonas putida
brenda
Lazic, J.; Spasic, J.; Francuski, D.; Tokic-Vujosevic, Z.; Nikodinovic-Runic, J.; Maslak, V.; Djokic, L.
Importance of N-terminal proline for the promiscuous activity of 4-oxalocrotonate tautomerase (4-OT)
J. Serb. Chem. Soc.
81
871-881
2016
Pseudomonas putida
-
brenda
van der Meer, J.Y.; Poddar, H.; Baas, B.J.; Miao, Y.; Rahimi, M.; Kunzendorf, A.; van Merkerk, R.; Tepper, P.G.; Geertsema, E.M.; Thunnissen, A.M.; Quax, W.J.; Poelarends, G.J.
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7
10911
2016
Pseudomonas putida (Q01468)
brenda
Radivojevic, J.; Minovska, G.; Senerovic, L.; OConnor, K.; Jovanovic, P.; Savic, V.; Tokic-Vujosevic, Z.; Nikodinovic-Runic, J.; Maslak, V.
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4
60502-60510
2014
Pseudomonas putida
-
brenda
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7
1745
2017
Staphylococcus aureus (Q6GH41), Staphylococcus aureus, Staphylococcus aureus MRSA252 (Q6GH41)
brenda