Information on EC 5.2.1.4 - Maleylpyruvate isomerase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
5.2.1.4
-
RECOMMENDED NAME
GeneOntology No.
Maleylpyruvate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-Maleylpyruvate = 3-fumarylpyruvate
show the reaction diagram
-, the mechanism of enzymic cis-trans isomerization involves an unstable transition complex of glutathione with maleylpyruvate, rather than the addition of glutathione across the double bond and its subsequent elimination
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cis-trans-isomerization
-
-
cis-trans-isomerization
-
-
cis-trans-isomerization
-
-
double bond
-
cis-trans-isomerization
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
3-phenylpropionate degradation
BRENDA
BRENDA
BRENDA
5-nitroanthranilate degradation
-
gentisate degradation I
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Tyrosine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
3-Maleylpyruvate cis-trans-isomerase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-maleylpyruvate cis-trans-isomerase
Q8NLC1
-
BagL
H6TG59
-
BagL
H6TG59
-
-
Isomerase, maleylpyruvate
-
-
-
-
maleylpyruvate isomerase
-
-
maleylpyruvate isomerase
-
-
-
maleylpyruvate isomerase
-
-
maleylpyruvate isomerase
Q8NLC1
-
maleylpyruvate isomerase
Corynebacterium glutamicum RES167
-
-
-
MDMPI
Q8NLC1
mycothiol dependent maleylpyruvate isomerase
MPI
-
-
-
-
mycothiol-dependent maleylpyruvate isomerase
-
-
mycothiol-dependent maleylpyruvate isomerase
-
-
-
NagL
-
-
-
ncgl2918 gene
Q8NLC1
-
thiol-dependent maleylpyruvate isomerase
H6TG59
-
thiol-dependent maleylpyruvate isomerase
H6TG59
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-77-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain CHC
-
-
Manually annotated by BRENDA team
Acinetobacter sp. CHC
strain CHC
-
-
Manually annotated by BRENDA team
strain 4CB/2-1
-
-
Manually annotated by BRENDA team
strain scl-2
-
-
Manually annotated by BRENDA team
Arthrobacter sp. 4CB/2-1
strain 4CB/2-1
-
-
Manually annotated by BRENDA team
strain scl-2
-
-
Manually annotated by BRENDA team
strain 410
-
-
Manually annotated by BRENDA team
Bacillus megaterium 410
strain 410
-
-
Manually annotated by BRENDA team
strain B4
-
-
Manually annotated by BRENDA team
strain PhphXAa-B, strain NP-1,strain SAL-1, strain SAL-6, strain SAL-8, strain SAL-11
-
-
Manually annotated by BRENDA team
strain B4
-
-
Manually annotated by BRENDA team
wild type; mshA-, mshB-, mshC-, mshD-deletion mutants
SWISSPROT
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
-
-
Manually annotated by BRENDA team
strain 16
-
-
Manually annotated by BRENDA team
Delftia acidovorans 16
strain 16
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus 6T-5
strain 6T-5
-
-
Manually annotated by BRENDA team
strain M5a1
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M5a1
strain M5a1
-
-
Manually annotated by BRENDA team
strain OA3
-
-
Manually annotated by BRENDA team
Moraxella sp. OA3
strain OA3
-
-
Manually annotated by BRENDA team
strain 3CS
-
-
Manually annotated by BRENDA team
Nocardia sp. 3CS
strain 3CS
-
-
Manually annotated by BRENDA team
gene bagL
UniProt
Manually annotated by BRENDA team
Rhodococcus erythropolis S1
strain S1
-
-
Manually annotated by BRENDA team
strain A81
-
-
Manually annotated by BRENDA team
Rhodococcus sp. A81
strain A81
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
H6TG59, -
BagL is a L-cysteine-dependent catabolic enzyme in microbial metabolism and is distinct member of DinB family, with a four-helix-bundle topology
evolution
-
BagL is a L-cysteine-dependent catabolic enzyme in microbial metabolism and is distinct member of DinB family, with a four-helix-bundle topology
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
H6TG59, -
-
-
-
?
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
Moraxella sp. OA3, Bacillus megaterium 410, Geobacillus stearothermophilus 6T-5, Rhodococcus sp. A81, Bacillus sp. B4, Nocardia sp. 3CS, Arthrobacter sp. 4CB/2-1, Acinetobacter sp. CHC, Delftia acidovorans 16
-
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
H6TG59
-
-
-
?
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
mutants lacking maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
pathway for the degradation of 3,5-xylenol
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme is involved in the pathway of 2-hydroxybenzoate degradation
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Rhodococcus erythropolis S1
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Pseudomonas putida NCIB9869
-
pathway for the degradation of 3,5-xylenol
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Klebsiella pneumoniae M5al
-
enzyme of the gentisate pathway, mutants lacking maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Klebsiella pneumoniae M5a1
-
enzyme of the gentisate pathway, mutants lacking maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited
-
-
-
3-maleylpyruvate +
3-fumarylpyruvate
show the reaction diagram
-, Q8NLC1
-
-
-
?
3-maleylpyruvate +
3-fumarylpyruvate
show the reaction diagram
Q8NLC1
-
-
-
?
Maleylacetoacetate
?
show the reaction diagram
-
-
-
-
-
Maleylacetoacetate
?
show the reaction diagram
-
very weak activity
-
-
-
Maleylacetoacetate
?
show the reaction diagram
Bacillus megaterium 410
-
-
-
-
-
Maleylacetoacetate
?
show the reaction diagram
Arthrobacter sp. 4CB/2-1
-
very weak activity
-
-
-
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
-
at pH 8.0
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
Corynebacterium glutamicum RES167
-
-, at pH 8.0
-
-
?
additional information
?
-
H6TG59, -
BagL is a thiol-dependent maleylpyruvate isomerase catalyzing the isomerization of maleylpyruvate to fumarylpyruvate with L-cysteine, cysteinylglycine, or glutathione, as its cofactor
-
-
-
additional information
?
-
H6TG59
BagL is a thiol-dependent maleylpyruvate isomerase catalyzing the isomerization of maleylpyruvate to fumarylpyruvate with L-cysteine, cysteinylglycine, or glutathione, as its cofactor
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
H6TG59, -
-
-
-
?
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
mutants lacking maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
pathway for the degradation of 3,5-xylenol
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
-
enzyme is involved in the pathway of 2-hydroxybenzoate degradation
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
-
-
-
-
?
3-Maleylpyruvate
?
show the reaction diagram
Rhodococcus erythropolis S1
-
enzyme of the gentisate pathway
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Pseudomonas putida NCIB9869
-
pathway for the degradation of 3,5-xylenol
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Klebsiella pneumoniae M5al
-
enzyme of the gentisate pathway, mutants lacking maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited
-
-
-
3-Maleylpyruvate
?
show the reaction diagram
Klebsiella pneumoniae M5a1
-
enzyme of the gentisate pathway, mutants lacking maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited
-
-
-
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
H6TG59
-
-
-
?
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
Corynebacterium glutamicum, Corynebacterium glutamicum RES167
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
mycothiol
-
dependent on
glutathione
-
dependent on reduced glutathione
additional information
-, Q8NLC1
MSH, mycothiol, 1D-myo-inosityl-1-(N-acetyl-L-cysteinyl)amido-2-deoxy-a-D-glucopyranoside, purified and identified by HPLC and mass spectrometric analysis
-
additional information
Q8NLC1
MSH, mycothiol, 1D-myo-inosityl-1-(N-acetyl-L-cysteinyl)amido-2-deoxy-a-D-glucopyranoside
-
additional information
H6TG59, -
L-cysteine, cysteinylglycine, or glutathione are possible cofactor, dependent on, cofactor kinetics, overview
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ni2+
H6TG59, -
activates
Zn2+
-, Q8NLC1
activating
Zn2+
Q8NLC1
probably required for activity
additional information
-, Q8NLC1
Mg2+, Ca2+, Cu2+, Ni2+, Mn2+ have no effect
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-, Q8NLC1
complete inhibitory at 10 mM
Fe3+
-, Q8NLC1
weak inhibitor
iodoacetamide
-
no inhibition
iodoacetamide
-
-
NEM
-
no inhibition
NEM
-
no inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-, Q8NLC1
weak activator at 1 mM
glutathione
-
reduced glutathione required
glutathione
-
no requirement for reduced glutathione
glutathione
-
no requirement for reduced glutathione
glutathione
-
reduced glutathione required
glutathione
-
no requirement for reduced glutathione
glutathione
-
reduced glutathione required
glutathione
-
no requirement for reduced glutathione
glutathione
-
glutathione-dependent enzyme: strain PhphXAa-B, strain NP-1, glutathione-independent enzyme: strain SAL-1, strain SAL-6, strain SAL-8, strain SAL-11
glutathione
-
reduced glutathione required
glutathione
-
no requirement for reduced glutathione
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
148.4
-
3-maleylpyruvate
-, Q8NLC1
-
0.344
-
maleylpyruvate
-
mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22C
0.346
-
maleylpyruvate
-
mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22C
0.407
-
maleylpyruvate
-
mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22C
0.566
-
maleylpyruvate
-
wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22C
0.69
-
maleylpyruvate
-
mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22C
1.029
-
maleylpyruvate
-
mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22C
2.355
-
maleylpyruvate
-
mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22C
3.339
-
maleylpyruvate
-
mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22C
6.517
-
maleylpyruvate
-
mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.54
-
maleylpyruvate
-
mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22C
1.06
-
maleylpyruvate
-
mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22C
11.11
-
maleylpyruvate
-
mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22C
13.45
-
maleylpyruvate
-
mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22C
22.59
-
maleylpyruvate
-
mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22C
31.47
-
maleylpyruvate
-
mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22C
51.45
-
maleylpyruvate
-
mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22C
101.3
-
maleylpyruvate
-
wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22C
120.9
-
maleylpyruvate
-
mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.316
-
maleylpyruvate
-
mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
1.579
-
maleylpyruvate
-
mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
2.063
-
maleylpyruvate
-
mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
21.84
-
maleylpyruvate
-
mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
21.96
-
maleylpyruvate
-
mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
27.31
-
maleylpyruvate
-
mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
91.31
-
maleylpyruvate
-
mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
175.1
-
maleylpyruvate
-
mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
179.1
-
maleylpyruvate
-
wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22C
3212
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
-
-
strain RES167-delta-ncg12921 (fragment of DNA encoding for amino acids 52-243 of Ncg12921 deleted)
420
-
-
strain RES167 (restriction-deficient mutant of ATCC13032)
540
-
-
strain RES167-delta-ncg12921/pMXJ19-ncg12921 (fragment of DNA encoding for amino acids 52-243 of Ncg12921 deleted and complementation of Ncg12921 generated by a plasmid carrying Ncg12921)
8700
-
-
recombinant protein expressed in Escherichia coli
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
8
-
-
8
-
H6TG59, -
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9
-
degradation of isocarbophos and organophosphate pesticides by scl-2
6
7.6
-
activity at pH 6.0 is 60% of the activity at pH 7.6
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
H6TG59, -
assay at
35
-
-
degradation of isocarbophos and organophosphate pesticides by scl-2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Klebsiella pneumoniae M5al, Klebsiella pneumoniae M5a1
-
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M5al, Klebsiella pneumoniae M5a1
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28000
-
Q8NLC1
SDS-PAGE, gel filtration
29000
-
-
gel filtration
30000
-
-
gel filtration
32000
-
-
SDS-PAGE
33000
-
-, Q8NLC1
SDS-PAGE
34000
-
-, Q8NLC1
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homodimer
H6TG59, -
-
homodimer
-
-
-
monomer
-
1 * 25000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-, Q8NLC1
1 x 33000, SDS-Page
monomer
-
1 * 30000, SDS-PAGE
-
additional information
H6TG59, -
sequence analysis and homology modeling
additional information
-
sequence analysis and homology modeling
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
of the wild type and one mutated enzyme (H52A), enzyme contains two domains
Q8NLC1
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cell extracts are prepared
-
of the recombinant enzyme
-, Q8NLC1
of the recombinant wild type and mutant enzymes
Q8NLC1
recombinant His6-tagged enzyme to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
H6TG59, -
Ni-NTA column chromatography and gel filtration
-
Ni-NTA agarose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
transformation into Escherichia coli 5K
-
gene bagL, DNA and amino acid sequence determination and analysis, phylogenetic analysis, comparison of genetic organization of gentisate catabolic gene clusters, recombinant expression of the N-terminall His6-tagged enzyme in Escherichia coli strain BL21(DE3)
H6TG59, -
expression in Escherichia coli
-
N-terminal His-tagged wild type enzyme and mutants are expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli Rosetta (DE3) pLysS cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the bag cluster is highly transcribed in 3-hydroxybenzoateinduced cells of strain NyZ101
H6TG59, -
the bag cluster is highly transcribed in 3-hydroxybenzoateinduced cells of strain NyZ101
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C61A
Q8NLC1
site directed mutagenesis
D151A
Q8NLC1
site directed mutagenesis, completely inactive
E144A
Q8NLC1
site directed mutagenesis, completely inactive
E85A
Q8NLC1
site directed mutagenesis
H148A
Q8NLC1
site directed mutagenesis, completely inactive
H48A
Q8NLC1
site directed mutagenesis
H52A
Q8NLC1
site directed mutagenesis, completely inactive
N56A
Q8NLC1
site directed mutagenesis, completely inactive
R141A
Q8NLC1
site directed mutagenesis, completely inactive
R222A
Q8NLC1
site directed mutagenesis, completely inactive
R82A
Q8NLC1
site directed mutagenesis, partially inactive
S78A
Q8NLC1
site directed mutagenesis, almost completely inactive
W44A
Q8NLC1
site directed mutagenesis, completely inactive
Y76A
Q8NLC1
site directed mutagenesis, completely inactive
D102A
-
completely inactive
H104A
-
the mutant shows 15.25% catalytic efficiency compared to the wild type enzyme
H38A
-
completely inactive
N108A
-
the mutant shows 50.83% catalytic efficiency compared to the wild type enzyme
P53A
-
completely inactive
Q49A
-
the mutant shows 1.15% catalytic efficiency compared to the wild type enzyme
Q64A
-
completely inactive
R109A
-
the mutant shows 0.88% catalytic efficiency compared to the wild type enzyme
R110A
-
completely inactive
R176A
-
the mutant shows 12.2% catalytic efficiency compared to the wild type enzyme
R8A
-
the mutant shows 12.26% catalytic efficiency compared to the wild type enzyme
R8A/R176A
-
the mutant shows 0.18% catalytic efficiency compared to the wild type enzyme
S9A
-
completely inactive
T11A
-
the mutant shows 97.81% catalytic efficiency compared to the wild type enzyme
D102A
-
completely inactive
-
H104A
-
the mutant shows 15.25% catalytic efficiency compared to the wild type enzyme
-
Q64A
-
completely inactive
-
R176A
-
the mutant shows 12.2% catalytic efficiency compared to the wild type enzyme
-
S9A
-
completely inactive
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
degradation
-
the potential use of pure culture microbial cells for the cleanup of organophosphorus-pesticide-contaminated enviroments is highlighted, and the mechanisms for isocarbophos degradation are presented
degradation
-
the potential use of pure culture microbial cells for the cleanup of organophosphorus-pesticide-contaminated enviroments is highlighted, and the mechanisms for isocarbophos degradation are presented
-
medicine
-, Q8NLC1
mycothiol as target for clinical treatment