Information on EC 3.1.1.45 - carboxymethylenebutenolidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.1.1.45
-
RECOMMENDED NAME
GeneOntology No.
carboxymethylenebutenolidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dichlorobenzene degradation
-
-
3,4,6-trichlorocatechol degradation
-
-
3,5-dichlorocatechol degradation
-
-
3-chlorocatechol degradation I (ortho)
-
-
3-chlorocatechol degradation II (ortho)
-
-
4,5-dichlorocatechol degradation
-
-
4-chlorocatechol degradation
-
-
3-chlorocatechol degradation
-
-
Chlorocyclohexane and chlorobenzene degradation
-
-
Fluorobenzoate degradation
-
-
Toluene degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
4-carboxymethylenebut-2-en-4-olide lactonohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
76689-22-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
type I DLH: trans-dienelactone hydrolyse
-
-
Manually annotated by BRENDA team
type I DLH: trans-dienelactone hydrolyse
-
-
Manually annotated by BRENDA team
male beagle dogs
UniProt
Manually annotated by BRENDA team
strain DH5alpha
-
-
Manually annotated by BRENDA team
strain DH5alpha
-
-
Manually annotated by BRENDA team
male cynomolgus monkey
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
DLH type III
-
-
Manually annotated by BRENDA team
possesses only the trans-substrate isomer-specific enzyme form
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
1CP, Rhodococcus erythropolis 1CP
-
-
Manually annotated by BRENDA team
gene dlh; DSM1616
UniProt
Manually annotated by BRENDA team
gene dlh; DSM1616
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-oxoadipate enol-lactone + H2O
?
show the reaction diagram
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
show the reaction diagram
4-carboxymethylenebut-2-en-4-olide + H2O
?
show the reaction diagram
4-chloromuconolactone + H2O
maleylacetate + HCl
show the reaction diagram
-
-
-
-
?
4-fluoro-muconolactone + H2O
?
show the reaction diagram
4-fluoromuconolactone + H2O
maleylacetate + HF
show the reaction diagram
alpha-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
azilsartan medoxomil + H2O
azilsartan + ?
show the reaction diagram
candesartan cilexetil + H2O
candesartan + ?
show the reaction diagram
cis-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
show the reaction diagram
-
-
-
?
cis-2-chloro-5-methyldienelactone + H2O
2-chloro-5-methylmaleylacetate
show the reaction diagram
-
-
-
?
cis-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
show the reaction diagram
-
-
-
?
cis-4-carboxymethylenebut-2-chloro-2-en-4-olide + H2O
?
show the reaction diagram
-
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
show the reaction diagram
cis-4-carboxymethylenebut-2-methyl-2-en-4-olide + H2O
?
show the reaction diagram
-
-
-
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
show the reaction diagram
cis-dienelactone + H2O
maleylacetate
show the reaction diagram
dienelactone + H2O
maleylacetate
show the reaction diagram
E/Z-dienelactone + H2O
maleylacetate
show the reaction diagram
faropenem medoxomil + H2O
?
show the reaction diagram
-
-
-
-
?
lenampicillin + H2O
?
show the reaction diagram
-
-
-
-
?
olmesartan medoxomil + H2O
?
show the reaction diagram
-
-
-
-
?
olmesartan medoxomil + H2O
olmesartan + diacetyl
show the reaction diagram
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
protoanemonin + H2O
cis-acetylacrylate
show the reaction diagram
trans-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
show the reaction diagram
-
-
-
?
trans-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
show the reaction diagram
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
show the reaction diagram
trans-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
show the reaction diagram
-
-
-
?
trans-cinnamoyl imidazole + H2O
trans-cinnamate + imidazole
show the reaction diagram
-
esterase activity
-
-
?
trans-dienelactone + H2O
maleylacetate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-carboxymethylene-but-2-ene-4-olide + H2O
(2E)-4-oxohex-2-enedioic acid
show the reaction diagram
4-carboxymethylenebut-2-en-4-olide + H2O
?
show the reaction diagram
4-chloromuconolactone + H2O
maleylacetate + HCl
show the reaction diagram
-
-
-
-
?
azilsartan medoxomil + H2O
azilsartan + ?
show the reaction diagram
candesartan cilexetil + H2O
candesartan + ?
show the reaction diagram
cis-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
show the reaction diagram
-
-
-
?
cis-2-chloro-5-methyldienelactone + H2O
2-chloro-5-methylmaleylacetate
show the reaction diagram
-
-
-
?
cis-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
show the reaction diagram
-
-
-
?
cis-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
show the reaction diagram
-
reaction is part of the degradation of dichloromethylcatechols as central intermediates in the degradation of dichlorotoluenes
-
?
cis-dienelactone + H2O
maleylacetate
show the reaction diagram
dienelactone + H2O
maleylacetate
show the reaction diagram
olmesartan medoxomil + H2O
olmesartan + diacetyl
show the reaction diagram
trans-2-chloro-3-methyldienelactone + H2O
2-chloro-3-methylmaleylacetate
show the reaction diagram
-
-
-
?
trans-3-chloro-2-methyldienelactone + H2O
3-chloro-2-methylmaleylacetate
show the reaction diagram
-
-
-
?
trans-5-chloro-2-methyldienelactone + H2O
5-chloro-2-methylmaleylacetate
show the reaction diagram
-
-
-
?
trans-dienelactone + H2O
maleylacetate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
78% inhibition at 5 mM
bis-p-nitrophenylphosphate
-
weak inhibitor
Cu2+
-
34% remaining activity after 5 min, 1 mM
dienelactam
-
diethyl dicarbonate
71% inhibition at 5 mM
diisopropylfluorophosphate
complete inhibition at 0.01 mM
Hg2+
-
6% remaining activity after 5 min, 1 mM
HgCl2
92% inhibition at 5 mM
o-phenanthroline
-
55% remaining activity after 5 min, 18% remaining activity after 60 min, 1 mM
p-chloromercuribenzoate
Paraoxon
complete inhibition at 5 mM
phenylmethylsulfonyl fluoride
-
PMSF, mimics the transition state of the reaction
PMSF
complete inhibition at 0.01 mM
protoanemonin
-
competitive inhibitor of the transformation of cis-dienelactone
succinate
-
reversible inhibitory effect
Zn2+
-
below 5% remaining activity after 5 min, 1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chlorocatechols
-
growth on chlorocatechols induce the trans-dienelactone hydrolase activity by 6fold
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
4-fluoromuconolactone
-
pH 7.5, 25°C
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
0.415
protoanemonin
-
-
0.015 - 9.9
trans-4-Carboxymethylenebut-2-en-4-olide
0.1017 - 0.55
trans-dienelactone
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
4-carboxymethylenebut-2-en-4-olide
-
-
1630 - 1633
4-fluoromuconolactone
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
-
-
-
0.63 - 14
E-dienelactone
0.24 - 138
p-nitrophenyl acetate
2.08
protoanemonin
-
-
2.67 - 15
trans-4-Carboxymethylenebut-2-en-4-olide
2650 - 15100
trans-dienelactone
0.18 - 19
Z-dienelactone
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0925
trans-dienelactone
pH 5.0, 60°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
after growth with benzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.02
-
substrate trans-dienelactone, crude enzyme extract of cells induced by 4-chlorobenzenesulfonic acid
0.021
-
Alcaligenes eutrophus 335 after growth with 4-hydroxy-benzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.025
-
Alcaligenes eutrophus 335 after growth with benzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.031
-
Alcaligenes eutrophus 335 after growth with succinate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.047
-
after growth with succinate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.055
-
after growth with 4-fluorobenzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.065
-
after growth with 4-fluorobenzoate, substrate cis-4-carboxymethylenebut-2-en-4-olide
0.18
-
Alcaligenes eutrophus JMP222 after growth with 4-fluorobenzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.29
-
Alcaligenes eutrophus JMP134 after growth with 4-fluorobenzoate, substrate cis-4-carboxymethylenebut-2-en-4-olide
0.53
-
Alcaligenes eutrophus JMP134 after growth with 4-fluorobenzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
0.58
-
substrate protoanemonin
0.61
-
crude enzyme extract from wild-type strain Ralstonia eutropha JMP134
1.4
-
Alcaligenes eutrophus JMP134 after growth with 2,4-dichlorophenoxy-acetate, substrate cis-4-carboxymethylenebut-2-en-4-olide
1.96
-
crude enzyme extract from recombinant strain Ralstonia eutropha JMP222
2
-
Alcaligenes eutrophus JMP134 after growth with 2,4-dichlorophenoxy-acetate, substrate trans-4-carboxymethylenebut-2-en-4-olide
4.6
-
Alcaligenes eutrophus 335 after growth with 4-fluorobenzoate, substrate trans-4-carboxymethylenebut-2-en-4-olide
29
-
strep-tagged protein, contains 1.9 mol of Zn2+, less than 0.1 mol of Mn2+, and 1.1 mol Ni2+ per mol of subunit
34
-
recombinant protein, contains 2.3 mol Zn2+, 0.8 mol Mn2+, and less than 0.1 mol Ni2+ per mol of subunit
58.8
-
substrate cis-4-carboxymethylenebut-2-en-4-olide
190
-
purified enzyme, substrate 4-fluoromuconolactone
710
-
purified enzyme, substrate trans-dienelactone
990
wild-type enzyme, substrate trans-dienelactone, pH 5.0, 60°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
assay for determination of pH-dependence of the activity
6.5
-
assay at
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.1
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
standard condition
55
-
assay for determination of temperature-dependence of the activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
assay range
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
-
transcript detected by RT-PCR
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25400 - 25800
27300
-
calculated of the clcD gene product
28000
-
AC866, 1 * 28000, SDS-PAGE
28500
-
gel filtration and nondenaturing PAGE
29000
SDS-PAGE, gel filtration and MALDI TOF mass spectrometry, recombinant enzyme
36940
-
calculated molecular weight
37000
-
determined by SDS-PAGE
58000
-
Alcaligenes eutrophus 335 and JMP222, gel filtration
85000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
-
C60S DLH; x-ray crystallographic structure at 2.8 A resolution
-
inhibitor, dienelactam, bound to DLH C123S
-
refined crystal structure at 1.8 A resolution
-
refined crystal structure of DLH at 1.8 A, C123S DLH at 2.2 A, C123A at 2.0 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
most stable around, decreasing faster towards lower than towards higher pH values
94359
7 - 7.2
-
highest stability at
94361
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
purified enzyme, 50% activity remaining after 50 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
(NH4)2SO4, 0.1-0.8 M, prevented the strong decline of activity
-
the purified enzyme shows high stability against denaturing agents, including various detergents, urea, and organic solvents
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 5 months, specific activity decreases from 217 to 65 U/mg
-
20°C, sodium succinate, pH 5, perfectly stable during incubation overnight
-
4°C, 20 mM Tris-HCl, pH 7.4, 10 micromol dithiothreitol, stable for over 6 months
-
4°C, 50 mM Tris-HCl, pH 7.2, 0.1 mM dithiothreitol, 0.5 M (NH4)2SO4, stable for over 3 months
-
4°C, converted to microcrystals, ammonium sulfate to 30% saturation, stable for more than 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-chlorobenzoate-grown cells
-
3-chlorobenzoate-grown cells; C123A DLH; C123S DLH
-
3-chlorobenzoate-grown cells; C123S DLH
-
native enzyme partially by anion exchange chromatography
-
partially
-
purified from human liver and intestinal cytosol using successive column chromatography
-
recombinant and wild-type trans-DLH are purified from cell extracts of Escherichia coli XL10-GOLD and Pseudomonas reinekei by subsequent anionic exchange, hydrophobic interaction, gel filtration and anionic exchange chromatography, the strep-tagged recombinant protein is purified using a Strep-Tactin Sepharose column
-
recombinant enzyme 150fold from Escherichia coli strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, dialysis, and another anion exchange chromatography
RW10 partial
-
subcellular fractionation from liver and intestine, recombinant tagged mutant enzymes by affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AC866 expression in Escherichia coli and Pseudomonas putida
-
expressed as a strep-tagged trans-DLH fusion protein in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli and Pseudomonas putida
-
expression of the enzyme encoded by gene tfdE in a module I of genes tfdC, tfdD, tfdE, and tfdF organized in one plasmid, functional expression in Ralstonia eutropha JMP222 and in Pseudomonas putida KT2442, 2 strains able to grow on 3-chlorobenzoate
-
gene dlh, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
into pGEM-T Easy and subsequently into pASK-IBA7plus for expression of the protein in Escherichia coli XL10-GOLD cells
-
recombinant expression of tagged mutant enzymes, semiquantitative tissue-specific expression analysis of wild-type and mutant enzymes
-
recombinantly expressed in mammalian cells and in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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/A205D/A229V
-
222% activity towards alpha-naphthyl acetate compared with the wild type enzyme; 224% activity towards alpha-naphthyl acetate compared with the wild type enzyme; 230% 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
C132A
-
mutant shows a drastic reduction of the olmesartan medoxomil-hydrolyzing activity; mutant shows a low activity, 30% of wild-type
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
C123A
-
inactive
C60S
-
no reduction in activity
D171N
-
no detectable activity
E36A
-
no detectable activity
D107A
-
mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
D107A/H111A
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mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
E294A
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mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
H111A
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mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
H281A
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mutation of a residue in the putative metal-binding site of trans-DLH results in a drastic decrease in activity
Q105A
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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
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site-directed mutagenesis, almost inactive mutant
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S102A
-
site-directed mutagenesis, the mutant is 3-5fold less active than the wild-type enzyme
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S103A
-
site-directed mutagenesis, 20% reduced activity compared to the wild-type enzyme
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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
-
additional information
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to evaluate the metal dependence of trans-DLH, a strep-tagged protein is purified
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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enzyme serves as a bioactivating hydrolase of olmesartan medoxomil, hydrolyzing the ester bond of the pro-drug type xenobiotics
Show AA Sequence (1486 entries)
Please use the Sequence Search for a specific query.