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 hide
5.2.1.4
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RECOMMENDED NAME
GeneOntology No.
Maleylpyruvate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis-trans-isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-phenylpropionate degradation
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5-nitroanthranilate degradation
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gentisate degradation I
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Metabolic pathways
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Microbial metabolism in diverse environments
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Tyrosine metabolism
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SYSTEMATIC NAME
IUBMB Comments
3-Maleylpyruvate cis-trans-isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-77-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CHC
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Manually annotated by BRENDA team
strain CHC
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Manually annotated by BRENDA team
strain 4CB/2-1
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Manually annotated by BRENDA team
strain scl-2
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Manually annotated by BRENDA team
strain 410
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Manually annotated by BRENDA team
strain 410
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-
Manually annotated by BRENDA team
strain B4
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
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Manually annotated by BRENDA team
strain 16
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Manually annotated by BRENDA team
strain 16
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Manually annotated by BRENDA team
strain 6T-5
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Manually annotated by BRENDA team
strain M5a1
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Manually annotated by BRENDA team
strain OA3
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Manually annotated by BRENDA team
strain OA3
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain 3CS
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Manually annotated by BRENDA team
strain 3CS
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Manually annotated by BRENDA team
gene bagL
UniProt
Manually annotated by BRENDA team
gene bagL
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain S1
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Manually annotated by BRENDA team
strain S1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain A81
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
3-Maleylpyruvate
?
show the reaction diagram
3-maleylpyruvate +
3-fumarylpyruvate
show the reaction diagram
Maleylacetoacetate
?
show the reaction diagram
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
additional information
?
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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
3-Maleylpyruvate
3-Fumarylpyruvate
show the reaction diagram
3-Maleylpyruvate
?
show the reaction diagram
Maleylpyruvate
Fumarylpyruvate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
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dependent on reduced glutathione
mycothiol
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dependent on
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
complete inhibitory at 10 mM
iodoacetamide
iodoacetate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
weak activator at 1 mM
glutathione
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
148.4
3-maleylpyruvate
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0.344 - 6.517
maleylpyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54 - 120.9
maleylpyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.316 - 179.1
maleylpyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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strain RES167-delta-ncg12921 (fragment of DNA encoding for amino acids 52-243 of Ncg12921 deleted)
420
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strain RES167 (restriction-deficient mutant of ATCC13032)
540
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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
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recombinant protein expressed in Escherichia coli
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
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degradation of isocarbophos and organophosphate pesticides by scl-2
6 - 7.6
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activity at pH 6.0 is 60% of the activity at pH 7.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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degradation of isocarbophos and organophosphate pesticides by scl-2
PDB
SCOP
CATH
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
SDS-PAGE, gel filtration
29000
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gel filtration
30000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
of the wild type and one mutated enzyme (H52A), enzyme contains two domains
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cell extracts are prepared
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Ni-NTA agarose column chromatography
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Ni-NTA column chromatography and gel filtration
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of the recombinant enzyme
of the recombinant wild type and mutant enzymes
recombinant His6-tagged enzyme to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) pLysS cells
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expression in Escherichia coli
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)
N-terminal His-tagged wild type enzyme and mutants are expressed in Escherichia coli BL21(DE3) cells
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transformation into Escherichia coli 5K
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the bag cluster is highly transcribed in 3-hydroxybenzoateinduced cells of strain NyZ101
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C61A
site directed mutagenesis
D151A
site directed mutagenesis, completely inactive
E144A
site directed mutagenesis, completely inactive
E85A
site directed mutagenesis
H148A
site directed mutagenesis, completely inactive
H48A
site directed mutagenesis
H52A
site directed mutagenesis, completely inactive
N56A
site directed mutagenesis, completely inactive
R141A
site directed mutagenesis, completely inactive
R222A
site directed mutagenesis, completely inactive
R82A
site directed mutagenesis, partially inactive
S78A
site directed mutagenesis, almost completely inactive
W44A
site directed mutagenesis, completely inactive
Y76A
site directed mutagenesis, completely inactive
D102A
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completely inactive
H104A
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the mutant shows 15.25% catalytic efficiency compared to the wild type enzyme
H38A
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completely inactive
N108A
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the mutant shows 50.83% catalytic efficiency compared to the wild type enzyme
P53A
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completely inactive
Q49A
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the mutant shows 1.15% catalytic efficiency compared to the wild type enzyme
Q64A
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completely inactive
R109A
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the mutant shows 0.88% catalytic efficiency compared to the wild type enzyme
R110A
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completely inactive
R176A
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the mutant shows 12.2% catalytic efficiency compared to the wild type enzyme
R8A
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the mutant shows 12.26% catalytic efficiency compared to the wild type enzyme
R8A/R176A
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the mutant shows 0.18% catalytic efficiency compared to the wild type enzyme
S9A
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completely inactive
T11A
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the mutant shows 97.81% catalytic efficiency compared to the wild type enzyme
D102A
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completely inactive
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H104A
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the mutant shows 15.25% catalytic efficiency compared to the wild type enzyme
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Q64A
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completely inactive
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R176A
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the mutant shows 12.2% catalytic efficiency compared to the wild type enzyme
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S9A
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completely inactive
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
medicine
mycothiol as target for clinical treatment
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