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3-oxoadipate enol-lactone + H2O
?
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
4-carboxymethylenebut-2-en-4-olide + H2O
?
4-chloromuconolactone + H2O
maleylacetate + HCl
-
-
-
-
?
4-fluoro-muconolactone + H2O
?
4-fluoromuconolactone + H2O
maleylacetate + HF
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
alpha-naphthyl acetate + H2O
1-naphthol + acetate
azilsartan medoxomil + H2O
azilsartan + ?
candesartan cilexetil + H2O
candesartan + ?
cis-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
-
-
-
?
cis-2-chloro-5-methyldienelactone + H2O
2-chloro-5-methylmaleylacetate
-
-
-
?
cis-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
-
-
-
?
cis-4-carboxymethylenebut-2-chloro-2-en-4-olide + H2O
?
-
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
cis-4-carboxymethylenebut-2-methyl-2-en-4-olide + H2O
?
-
-
-
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
cis-dienelactone + H2O
maleylacetate
dienelactone + H2O
maleylacetate
E/Z-dienelactone + H2O
maleylacetate
faropenem medoxomil + H2O
?
-
-
-
-
?
lenampicillin + H2O
?
-
-
-
-
?
olmesartan medoxomil + H2O
?
-
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
protoanemonin + H2O
cis-acetylacrylate
trans-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
-
-
-
?
trans-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
trans-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
-
-
-
?
trans-cinnamoyl imidazole + H2O
trans-cinnamate + imidazole
-
esterase activity
-
-
?
trans-dienelactone + H2O
maleylacetate
Z-dienelactone + H2O
maleyl acetate
additional information
?
-
3-oxoadipate enol-lactone + H2O
?
-
Alcaligenes eutrophus JMP134 not a substrate
-
-
?
3-oxoadipate enol-lactone + H2O
?
-
Alcaligenes eutrophus 335 and JMP222
-
-
?
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
-
third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate
-
-
?
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
-
third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate
-
-
?
4-carboxymethylenebut-2-en-4-olide + H2O
?
-
the enzyme is one of the enzymes of the halocatechol branch of the beta-ketoadipate pathway, a complex set of catabolic reactions used by bacteria for utilization of aromatic compounds
-
-
?
4-carboxymethylenebut-2-en-4-olide + H2O
?
-
dienelactone hydrolase catalyzes a step in the metabolic conversion of chlorocatechols to beta-ketoadipate
-
-
?
4-fluoro-muconolactone + H2O
?
-
-
-
-
?
4-fluoro-muconolactone + H2O
?
-
-
-
-
?
4-fluoro-muconolactone + H2O
?
-
AC866
-
-
?
4-fluoromuconolactone + H2O
maleylacetate + HF
-
-
-
?
4-fluoromuconolactone + H2O
maleylacetate + HF
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
E2RF91
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
E2RF91
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
not a substrate to a significant extent
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
not a substrate to a significant extent
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
Alcaligenes eutrophus JPM134
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222: not a substrate to a significant extent
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
ir
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
Pseudomonas putida AC866
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
Pseudomonas putida RW10 not a substrate to a significant extent
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
-
-
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
-
reaction is part of the degradation of dichloromethylcatechols as central intermediates in the degradation of dichlorotoluenes
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
best substrate
-
?
cis-dienelactone + H2O
maleylacetate
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
best substrate
-
?
dienelactone + H2O
maleylacetate
-
enzyme is involved in the degradation of chlorocatechols resulting from growth on from 3-chlorobenzoate and 2,4-dichlorophenoxyacetate
-
?
dienelactone + H2O
maleylacetate
-
enzyme is involved in the degradation of chlorocatechols resulting from growth on from 3-chlorobenzoate and 2,4-dichlorophenoxyacetate
-
?
dienelactone + H2O
maleylacetate
-
-
-
?
dienelactone + H2O
maleylacetate
-
-
-
?
E/Z-dienelactone + H2O
maleylacetate
-
the reaction is reversible when performed by the mutant enzyme C123S
-
?
E/Z-dienelactone + H2O
maleylacetate
-
the reaction is reversible when performed by the mutant enzyme C123S
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
E2RF91
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
esterase activity
-
-
?
protoanemonin + H2O
cis-acetylacrylate
-
activity of cis-dienelactone hydrolase with 50 microM protoanemonin is 0.08% of that observed with 50 microM cis-dienelactone, cis-4-carboxymethylenebut-2-en-4-olide
-
-
?
protoanemonin + H2O
cis-acetylacrylate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
not a substrate to a significant extent
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
ir
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
-
not a substrate to a significant extent
-
-
?
trans-dienelactone + H2O
maleylacetate
-
specific for the trans-isomer, no activity with the cis-isomer
-
-
?
trans-dienelactone + H2O
maleylacetate
-
-
-
-
?
trans-dienelactone + H2O
maleylacetate
-
-
-
-
?
trans-dienelactone + H2O
maleylacetate
-
very low activity with the cis-isomer
-
?
trans-dienelactone + H2O
maleylacetate
-
degradation of chlorosalicylates via chlorocatechols to 3-oxoadipate via maleylacetate, pathway overview
-
?
trans-dienelactone + H2O
maleylacetate
-
-
-
-
?
trans-dienelactone + H2O
maleylacetate
-
very low activity with the cis-isomer
-
?
trans-dienelactone + H2O
maleylacetate
-
degradation of chlorosalicylates via chlorocatechols to 3-oxoadipate via maleylacetate, pathway overview
-
?
trans-dienelactone + H2O
maleylacetate
the enzyme displays substrate specificities toward trans-dienelactone, not cis-isomer
-
-
?
trans-dienelactone + H2O
maleylacetate
the enzyme displays substrate specificities toward trans-dienelactone, not cis-isomer
-
-
?
Z-dienelactone + H2O
maleyl acetate
-
-
-
-
?
Z-dienelactone + H2O
maleyl acetate
-
-
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
muconolactone is not hydrolyzed to a significant extent
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
natural function is not in the degradation of haloaromatic compounds, the normal substrate might well be one of the more complex natural compounds with a dienelactone structure, or it could also be an intermediate of some other metabolic pathway
-
-
?
additional information
?
-
E2RF91
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of 4-chlorobenzenesulfonic acid, 4CBSA, the major polar by-product of the chemical synthesis of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl) ethane, DDT, overview, 4-chlorobenzenesulfonic acid catabolic pathway, overview
-
-
?
additional information
?
-
-
no activity with protoanemonin
-
-
?
additional information
?
-
-
muconolactone is not hydrolyzed to a significant extent
-
-
?
additional information
?
-
-
DLH unable to hydrolyze lactams which closely resemble its substrate, dienelactam is not a substrate, DLH has lost the ability to hydrolyze amides
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
substrate specificities differentiate among three types of this activity. Type I: extracts of Alcaligenes eutrophus 335, Alcaligenes eutrophus H16, Alcaligenes eutrophus JMP222 and Alcaligenes strain A7 convert trans-4-carboxymethylenebut-2-en-4-olide, trans-dienelactone, much faster than cis-isomer, type II: enzyme of Pseudomonas cepacia converts cis-dienelactone much faster, type III: enzyme of Alcaligenes eutrophus JMP134 and Pseudomonas strain B13 hydrolyze both dienelactones
-
-
?
additional information
?
-
-
substrate binding studies
-
-
?
additional information
?
-
-
it seems likely, that dienelactone hydrolase has the additional function of detoxification of minor amounts of protoanemonin that may be formed during chloroaromatic degradation
-
-
?
additional information
?
-
-
antibiotic protoanemonin is a poor substrate
-
?
additional information
?
-
-
the mutant C123S catalyzes the isomerase reaction which changes the E-isomer to Z-isomer and vice versa
-
?
additional information
?
-
-
antibiotic protoanemonin is no substrate
-
?
additional information
?
-
-
the mutant C123S catalyzes the isomerase reaction which changes the E-isomer to Z-isomer and vice versa
-
?
additional information
?
-
-
antibiotic protoanemonin is a poor substrate
-
?
additional information
?
-
-
antibiotic protoanemonin is no substrate
-
?
additional information
?
-
-
antibiotic protoanemonin is a poor substrate
-
?
additional information
?
-
-
pathway overview
-
?
additional information
?
-
-
antibiotic protoanemonin is a poor substrate
-
?
additional information
?
-
-
pathway overview
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity with 2-methylmuconolactone, 4-methylmuconolactone
-
-
?
additional information
?
-
the enzyme is a typical dienelactone hydrolase belonging to alpha/beta hydrolase family and containing a catalytic triad composed of Cys151, Asp198, and His229 in the active site
-
-
?
additional information
?
-
the enzyme also shows carboxylesterase activity toward 4-nitrophenyl esters ranging from butyrate to laurate
-
-
?
additional information
?
-
the enzyme is a typical dienelactone hydrolase belonging to alpha/beta hydrolase family and containing a catalytic triad composed of Cys151, Asp198, and His229 in the active site
-
-
?
additional information
?
-
the enzyme also shows carboxylesterase activity toward 4-nitrophenyl esters ranging from butyrate to laurate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
4-carboxymethylenebut-2-en-4-olide + H2O
?
4-chloromuconolactone + H2O
maleylacetate + HCl
-
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
candesartan cilexetil + H2O
candesartan + ?
cis-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
-
-
-
?
cis-2-chloro-5-methyldienelactone + H2O
2-chloro-5-methylmaleylacetate
-
-
-
?
cis-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
-
-
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
-
reaction is part of the degradation of dichloromethylcatechols as central intermediates in the degradation of dichlorotoluenes
-
?
cis-dienelactone + H2O
maleylacetate
dienelactone + H2O
maleylacetate
olmesartan medoxomil + H2O
olmesartan + diacetyl
trans-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
-
-
-
?
trans-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
-
-
-
?
trans-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
-
-
-
?
trans-dienelactone + H2O
maleylacetate
additional information
?
-
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
-
third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate
-
-
?
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
-
third enzyme of the halocatechol branch of the beta-ketoadipate pathway, catalyses the hydrolysis of both, (E) and (Z) dienelactone to maleyl acetate
-
-
?
4-carboxymethylenebut-2-en-4-olide + H2O
?
-
the enzyme is one of the enzymes of the halocatechol branch of the beta-ketoadipate pathway, a complex set of catabolic reactions used by bacteria for utilization of aromatic compounds
-
-
?
4-carboxymethylenebut-2-en-4-olide + H2O
?
-
dienelactone hydrolase catalyzes a step in the metabolic conversion of chlorocatechols to beta-ketoadipate
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
E2RF91
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
E2RF91
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
candesartan cilexetil + H2O
candesartan + ?
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
-
-
?
cis-dienelactone + H2O
maleylacetate
-
-
-
?
dienelactone + H2O
maleylacetate
-
enzyme is involved in the degradation of chlorocatechols resulting from growth on from 3-chlorobenzoate and 2,4-dichlorophenoxyacetate
-
?
dienelactone + H2O
maleylacetate
-
enzyme is involved in the degradation of chlorocatechols resulting from growth on from 3-chlorobenzoate and 2,4-dichlorophenoxyacetate
-
?
dienelactone + H2O
maleylacetate
-
-
-
?
dienelactone + H2O
maleylacetate
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
E2RF91
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
-
-
-
?
trans-dienelactone + H2O
maleylacetate
-
specific for the trans-isomer, no activity with the cis-isomer
-
-
?
trans-dienelactone + H2O
maleylacetate
-
-
-
-
?
trans-dienelactone + H2O
maleylacetate
-
degradation of chlorosalicylates via chlorocatechols to 3-oxoadipate via maleylacetate, pathway overview
-
?
trans-dienelactone + H2O
maleylacetate
-
degradation of chlorosalicylates via chlorocatechols to 3-oxoadipate via maleylacetate, pathway overview
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
natural function is not in the degradation of haloaromatic compounds, the normal substrate might well be one of the more complex natural compounds with a dienelactone structure, or it could also be an intermediate of some other metabolic pathway
-
-
?
additional information
?
-
E2RF91
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
-
the enzyme is involved in degradation of 4-chlorobenzenesulfonic acid, 4CBSA, the major polar by-product of the chemical synthesis of 1,1,1-trichloro-2,2-bis-(4-chlorophenyl) ethane, DDT, overview, 4-chlorobenzenesulfonic acid catabolic pathway, overview
-
-
?
additional information
?
-
-
it seems likely, that dienelactone hydrolase has the additional function of detoxification of minor amounts of protoanemonin that may be formed during chloroaromatic degradation
-
-
?
additional information
?
-
-
antibiotic protoanemonin is no substrate
-
?
additional information
?
-
-
antibiotic protoanemonin is no substrate
-
?
additional information
?
-
-
pathway overview
-
?
additional information
?
-
-
pathway overview
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
the activity with prodrug-type angiotensin II type 1 receptor blocker differs in a tissue-dependent and subcellular-dependent manner, overview
-
-
?
additional information
?
-
the enzyme is a typical dienelactone hydrolase belonging to alpha/beta hydrolase family and containing a catalytic triad composed of Cys151, Asp198, and His229 in the active site
-
-
?
additional information
?
-
the enzyme is a typical dienelactone hydrolase belonging to alpha/beta hydrolase family and containing a catalytic triad composed of Cys151, Asp198, and His229 in the active site
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.2
4-fluoromuconolactone
-
pH 7.5, 25Ā°C
0.012 - 0.014
4-nitrophenyl acetate
0.02 - 0.074
Alpha-naphthyl acetate
0.0022
cis-4-carboxymethylenebut-2-chloro-2-en-4-olide
-
-
0.0281 - 0.59
cis-4-carboxymethylenebut-2-en-4-olide
0.31
cis-4-carboxymethylenebut-2-methyl-2-en-4-olide
-
-
0.28
faropenem medoxomil
-
recombinant CMBL, Vmax: 16.4 nmol/min/mg
0.063
lenampicillin
-
recombinant CMBL, Vmax: 4 nmol/min/mg
0.16 - 0.48
olmesartan medoxomil
0.007 - 0.021
p-nitrophenyl acetate
0.015 - 9.9
trans-4-Carboxymethylenebut-2-en-4-olide
0.1017 - 0.55
trans-dienelactone
additional information
additional information
-
0.012
4-nitrophenyl acetate
mutant Q35H/F38L/C123S/Y145C/N154D/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.013
4-nitrophenyl acetate
mutant Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.013
4-nitrophenyl acetate
mutant Q35H/F38L/C123S/Y145C/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.013
4-nitrophenyl acetate
mutant Q35H/F38L/Q110L/C123S/Y145C/N154D/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.014
4-nitrophenyl acetate
mutant Q35H/F38L/Q110L/C123S/Y137C/Y145C/N154D/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.014
4-nitrophenyl acetate
mutant Q35H/F38L/Q110L/C123S/Y145C/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.02
Alpha-naphthyl acetate
-
E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0
0.023
Alpha-naphthyl acetate
-
E36D,C123S mutant enzyme, pH 7.0
0.032
Alpha-naphthyl acetate
-
E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0
0.074
Alpha-naphthyl acetate
-
C123S mutant enzyme, pH 7.0
0.0281
cis-4-carboxymethylenebut-2-en-4-olide
-
-
0.14
cis-4-carboxymethylenebut-2-en-4-olide
-
Alcaligenes eutrophus JMP134, cell-free extract, not with purified enzyme
0.381
cis-4-carboxymethylenebut-2-en-4-olide
-
-
0.4
cis-4-carboxymethylenebut-2-en-4-olide
-
-
0.59
cis-4-carboxymethylenebut-2-en-4-olide
-
-
0.16
olmesartan medoxomil
-
native enzyme from liver cytosol, Vmax: 19.7 nmol/min/mg
0.17
olmesartan medoxomil
-
recombinant CMBL, Vmax: 24.6 nmol/min/mg
0.19
olmesartan medoxomil
-
native enzyme from intestine cytosol, Vmax: 45 nmol/min/mg
0.23
olmesartan medoxomil
-
native enzyme from intestinal microsomes, Vmax: 6.76 nmol/min/mg
0.48
olmesartan medoxomil
-
native enzyme from liver microsomes, Vmax: 15 nmol/min/mg
0.007
p-nitrophenyl acetate
-
E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0
0.008
p-nitrophenyl acetate
-
E36D,C123S mutant enzyme, pH 7.0
0.008
p-nitrophenyl acetate
-
E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0
0.021
p-nitrophenyl acetate
-
C123S mutant enzyme, pH 7.0
0.015
trans-4-Carboxymethylenebut-2-en-4-olide
-
-
0.11
trans-4-Carboxymethylenebut-2-en-4-olide
-
Alcaligenes eutrophus JMP134, cell-free extract, not with purified enzyme
0.17
trans-4-Carboxymethylenebut-2-en-4-olide
-
-
0.22
trans-4-Carboxymethylenebut-2-en-4-olide
-
C60S DLH
1.8
trans-4-Carboxymethylenebut-2-en-4-olide
-
-
9.9
trans-4-Carboxymethylenebut-2-en-4-olide
-
C123S DLH
0.1017
trans-dienelactone
pH 5.0, 60Ā°C
0.48
trans-dienelactone
-
pH 7.5, 25Ā°C
0.55
trans-dienelactone
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
E2RF91
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics with other 4-nitrophenyl esters for carboxylesterase activity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30
4-carboxymethylenebut-2-en-4-olide
-
-
1630 - 1633
4-fluoromuconolactone
0.57 - 0.61
4-nitrophenyl acetate
0.24 - 120
Alpha-naphthyl acetate
19.8
cis-4-carboxymethylenebut-2-chloro-2-en-4-olide
-
-
15.4 - 817
cis-4-carboxymethylenebut-2-en-4-olide
4.95
cis-4-carboxymethylenebut-2-methyl-2-en-4-olide
-
-
0.24 - 138
p-nitrophenyl acetate
2.67 - 15
trans-4-Carboxymethylenebut-2-en-4-olide
2650 - 15100
trans-dienelactone
1630
4-fluoromuconolactone
-
pH 7.5, 25Ā°C
1633
4-fluoromuconolactone
-
pH 7.5, 25Ā°C
0.57
4-nitrophenyl acetate
mutant Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.58
4-nitrophenyl acetate
mutant Q35H/F38L/C123S/Y145C/N154D/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.58
4-nitrophenyl acetate
mutant Q35H/F38L/Q110L/C123S/Y145C/N154D/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.59
4-nitrophenyl acetate
mutant Q35H/F38L/C123S/Y145C/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.6
4-nitrophenyl acetate
mutant Q35H/F38L/Q110L/C123S/Y145C/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.61
4-nitrophenyl acetate
mutant Q35H/F38L/Q110L/C123S/Y137C/Y145C/N154D/E199G/S208G/G211D, pH 7.5, 25Ā°C
0.24
Alpha-naphthyl acetate
-
E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0
1.6
Alpha-naphthyl acetate
-
E36D,C123S mutant enzyme, pH 7.0
2.05
Alpha-naphthyl acetate
-
E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0
63.4
Alpha-naphthyl acetate
-
C123S mutant enzyme, pH 7.0
71.2
Alpha-naphthyl acetate
-
E36D,C123S mutant enzyme, pH 7.0
86.2
Alpha-naphthyl acetate
-
E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0
98.1
Alpha-naphthyl acetate
-
E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0
120
Alpha-naphthyl acetate
-
C123S mutant enzyme, pH 7.0
15.4
cis-4-carboxymethylenebut-2-en-4-olide
-
-
260
cis-4-carboxymethylenebut-2-en-4-olide
-
-
817
cis-4-carboxymethylenebut-2-en-4-olide
-
-
0.63
E-dienelactone
-
mutant C123S, pH 7.0, 24Ā°C
6.08
E-dienelactone
-
mutant C123S, pH 7.0, 24Ā°C
14
E-dienelactone
-
wild-type enzyme, pH 7.0, 24Ā°C
0.24
p-nitrophenyl acetate
-
E36D,C123S mutant enzyme, pH 7.0
2.9
p-nitrophenyl acetate
-
C123S mutant enzyme, pH 7.0
97.9
p-nitrophenyl acetate
-
E36D,C123S mutant enzyme, pH 7.0
107.7
p-nitrophenyl acetate
-
C123S mutant enzyme, pH 7.0
123
p-nitrophenyl acetate
-
E36D,R105H,C123S,G211D,K234N mutant enzyme, pH 7.0
126.8
p-nitrophenyl acetate
-
E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0
138
p-nitrophenyl acetate
-
E36D,C123S,A134S,S208G,A229V,K234R mutant enzyme, pH 7.0
2.67
trans-4-Carboxymethylenebut-2-en-4-olide
-
C123S DLH
9.17
trans-4-Carboxymethylenebut-2-en-4-olide
-
-
15
trans-4-Carboxymethylenebut-2-en-4-olide
-
C60S DLH
2650
trans-dienelactone
-
pH 7.5, 25Ā°C
9409
trans-dienelactone
pH 5.0, 60Ā°C
15100
trans-dienelactone
-
recombinant protein
0.18
Z-dienelactone
-
mutant C123S, pH 7.0, 24Ā°C
19
Z-dienelactone
-
wild-type enzyme, pH 7.0, 24Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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C123S
-
100% activity towards alpha-naphthyl acetate compared with the wild type enzyme
C123S/R206A
-
65% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36A/C123S
-
no activity activity towards alpha-naphthyl acetate
E36D
-
104% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S
-
183% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/A134S/S208G/A229V/K234R
-
256% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/A134T/A229V
-
164% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/A205D
-
217% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/A229V
-
187% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/F173A
-
no activity activity towards alpha-naphthyl acetate
E36D/C123S/G211D/A229V
-
172% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/G211D/K234N
-
205% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/R206T/A229V
-
122% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/R105H/C123S/G211D/K234N
-
233% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/R45Q/C123S
-
172% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/R45Q/C123S/A205D/A229V
-
148% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/R81A/C123S/R206A
-
114% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36N/C123S
-
140% activity towards alpha-naphthyl acetate compared with the wild type enzyme
C123S
-
100% activity towards alpha-naphthyl acetate compared with the wild type enzyme
-
E36A/C123S
-
no activity activity towards alpha-naphthyl acetate
-
E36D
-
104% activity towards alpha-naphthyl acetate compared with the wild type enzyme
-
E36D/R81A/C123S/R206A
-
114% activity towards alpha-naphthyl acetate compared with the wild type enzyme
-
E36N/C123S
-
140% activity towards alpha-naphthyl acetate compared with the wild type enzyme
-
A150T
site-directed mutagenesis, the mutant shows slightly higher Vmax with olmesartan medoxomil compared to the wild-type enzyme
Y155C
site-directed mutagenesis, the enzyme mutant is caused by a single nucleotide polymorphism rs35489000 and shows 50% reduced olmesartan medoxomil-hydrolase activity, slightly higher Km, and lower Vmax compared to the wild-type protein
C60S
-
no reduction in activity
D171N
-
no detectable activity
E36A
-
no detectable activity
Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/C123S/Y145C/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/C123S/Y145C/N154D/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/Q110L/C123S/Y137C/Y145C/N154D/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/Q110L/C123S/Y145C/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/Q110L/C123S/Y145C/N154D/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D
-
mutations do not influence the kinetic properties
-
Q35H/F38L/C123S/Y145C/E199G/S208G/G211D
-
mutations do not influence the kinetic properties
-
Q35H/F38L/C123S/Y145C/N154D/E199G/S208G/G211D
-
mutations do not influence the kinetic properties
-
Q35H/F38L/Q110L/C123S/Y145C/E199G/S208G/G211D
-
mutations do not influence the kinetic properties
-
D107A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
D107A/H111A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
E294A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
H111A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
H281A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
Q105A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
C151S
site-directed mutagenesis, almost inactive mutant
D198N
site-directed mutagenesis, almost inactive mutant
H229N
site-directed mutagenesis, almost inactive mutant
S102A
site-directed mutagenesis, the mutant is 3-5fold less active than the wild-type enzyme
S103A
site-directed mutagenesis, 20% reduced activity compared to the wild-type enzyme
S120A
site-directed mutagenesis, the mutant is 3-5fold less active than the wild-type enzyme
S139A
site-directed mutagenesis, the mutant is 3-5fold less active than the wild-type enzyme
S147A
site-directed mutagenesis, 20% reduced activity compared to the wild-type enzyme
S210A
site-directed mutagenesis, the mutant shows similar activity like the wild-type enzyme
H229N
-
site-directed mutagenesis, almost inactive mutant
-
S102A
-
site-directed mutagenesis, the mutant is 3-5fold less active than the wild-type enzyme
-
S103A
-
site-directed mutagenesis, 20% reduced activity compared to the wild-type enzyme
-
S120A
-
site-directed mutagenesis, the mutant is 3-5fold less active than the wild-type enzyme
-
S210A
-
site-directed mutagenesis, the mutant shows similar activity like the wild-type enzyme
-
E36D/C123S/A205D/A229V
-
222% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/A205D/A229V
-
224% activity towards alpha-naphthyl acetate compared with the wild type enzyme
E36D/C123S/A205D/A229V
-
230% activity towards alpha-naphthyl acetate compared with the wild type enzyme
C132A
-
mutant shows a drastic reduction of the olmesartan medoxomil-hydrolyzing activity
C132A
-
mutant shows a low activity, 30% of wild-type
C123S
-
-
C123S
-
burst kinetics with p-nitrophenyl acetate, 10% as active as DLH
C123S
-
maximal activity 20% that of the wild type protein
C123S
-
site-directed mutagenesis, mutation of the active site cysteine to a serine, giving a catalytic triad found in serine proteases, completely changes the catalytic activity to a dienelactone isomerase
C123S
-
site-directed mutagenesis, mutation of the active site cysteine to a serine, giving a catalytic triad found in serine proteases, completely changes the catalytic activity to a dienelactone isomerase
-
additional information
the surface mutations Q110L, Y137C and N154D do not influence the kinetic properties. Mutations Q110L and N154D have stabilizing effects, the Y137C mutation alone is destabilizing. The three mutations together increase the melting temperature by 3.4 degrees
additional information
-
the surface mutations Q110L, Y137C and N154D do not influence the kinetic properties. Mutations Q110L and N154D have stabilizing effects, the Y137C mutation alone is destabilizing. The three mutations together increase the melting temperature by 3.4 degrees
-
additional information
-
to evaluate the metal dependence of trans-DLH, a strep-tagged protein is purified
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