Information on EC 5.2.1.1 - Maleate isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.2.1.1
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RECOMMENDED NAME
GeneOntology No.
Maleate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Maleate = fumarate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis-trans-isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
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Microbial metabolism in diverse environments
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Nicotinate and nicotinamide metabolism
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nicotinate degradation I
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nicotinate degradation II
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nicotine degradation II (pyrrolidine pathway)
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nicotine degradation III (VPP pathway)
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citric acid cycle
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SYSTEMATIC NAME
IUBMB Comments
Maleate cis-trans-isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-74-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
T501
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Manually annotated by BRENDA team
T501
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene ro00478
UniProt
Manually annotated by BRENDA team
IFO3736
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Manually annotated by BRENDA team
IFO3736
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Maleate
Fumarate
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
Maleate
Fumarate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CO2
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increases activity by 20-30%
Fe2+
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increases activity by 20-30%
Mn2+
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increases activity by 20-30%
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bromoacetate
bromomaleate
weak inhibitor
cyanide
deoxycholate
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iodoacetamide
iodoacetate
N-bromosuccinimide
N-Chlorosuccinimide
NaCN
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0.6 mM, 20% inhibition
NaF
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0.6-3 mM, 18-45% inhibition
p-Chloromercuriphenylsulfonate
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p-Substituted mercuribenzoate
p-toluenesulfonchloramide
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1 mM, complete inhibition
Semicarbazide
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1 mM, weak inhibition
Sodium periodate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
dithiothreitol
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activates
Mercaptans
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00053 - 2.8
Maleate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00035 - 96.7
Maleate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 650
Maleate
575
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
bromomaleate
pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106.8
purified enzyme mutant MaiR-D48/49-304AA, pH 8.0, 40C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
activity range, recombinant mutant MaiR-D48/49-304AA
6.5 - 9.3
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about 50% of maximal activity at pH 6.5 and at pH 9.3
6.7 - 9.4
6.8 - 9.3
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about 50% of maximal activity at pH 6.8 and 9.3
7 - 9
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more than 75% of maximal activity at pH 7.0 and pH 9.0
7 - 9.3
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pH 7: about 60% of maximal activity, pH 9.3: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
recombinant mutant MaiR-D48/49-304AA
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
activity range, recombinant mutant MaiR-D48/49-304AA
30 - 60
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30C: about 60% of maximal activity, 60C: about 40% of maximal activity
30 - 70
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increase of activity from 30C to 70C
30 - 60
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30C: about 70% of maximal activity, 60C: about 70% of maximal activity
35 - 50
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about 50% of maximal activity at 35C and 50C
PDB
SCOP
CATH
ORGANISM
UNIPROT
Nocardia farcinica (strain IFM 10152)
Nocardia farcinica (strain IFM 10152)
Pseudomonas putida (strain S16)
Pseudomonas putida (strain S16)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26950
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x * 26950, calculation from nucleotide sequence
27971
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2 * 27971, calculation from nucleotide sequence
60000
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gel filtration
100000
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gel filtration, sedimentation velocity studies
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
im complex with maleate
purified recombinant wild-type alone, and mutant enzyme C200A in complex with substrate maleate, hanging-drop vapour-diffusion method, mixing of 15-20 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 2 mM DTT, with a reservoir solution containing 25% w/v PEG3,350 and 0.1 M Tris, pH 8.5, for the substrate-enzyme mutant complex, and 1.4 M (NH4)2SO4, 120 mM NaCl, and 0.1 M HEPES, pH 7.5, for the free wild-type enzyme, 14C, X-ray diffraction structure determination and analysis at 2.95 A and 2.10 A resolution, respectively
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 25
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pH 6, maximal stability in presence of small quantities of dithiothreitol
30
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15 min, stable below
45
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30 min, about 10% loss of activity
53
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30 min, complete inactivation
55 - 60
purified recombinant mutant MaiR-D48/49-304AA, 30 min, over 95% activity at 55C and about 50% activity at 60C remaining
57
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30 min, stable below
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crystallization can be accompanied by a 50% loss in activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme mutant MaiR-D48 shows high oxidative stability
728167
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, overnight, 10% loss of activity
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4C, 20% glycerol, 10 mM thioglycerol, 3 months, 70% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant mutant MaiR-D48/49-304AA 2.7fold from Escherichia coli strain Rosetta 2 (DE3) by ammonium sulfate fractionation, anion exchange chromatography, ultratfiltration, and gel filtration
recombinant N- and C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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gene ro00478, recombinant expression of wild-type and mutants in Escherichia coli Rosetta2 (DE3) pLysS
overexpression of N- and C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C194S
the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
C76S
the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
Y133F
the mutant shows decreased turnover and Km, but about wild type catalytic efficiency
C194A
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inactive
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C194S
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the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
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C76S
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the mutant displays more than 1000fold reduced turnover compared to the wild type enzyme
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Y133F
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the mutant shows decreased turnover and Km, but about wild type catalytic efficiency
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C200A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, substrate-binding structure: maleate can be found to exist inside a cavity of the enzyme, totally surrounded by the protein
C84A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
C200A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, substrate-binding structure: maleate can be found to exist inside a cavity of the enzyme, totally surrounded by the protein
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C84A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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M138C
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mutant enzyme shows 90% of the activity of the wild-type enzyme
M18C
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mutant enzyme shows 30% of the activity of the wild-type enzyme
M201C
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mutant enzyme shows 90% of the activity of the wild-type enzyme
M46C
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mutant enzyme shows 30% of the activity of the wild-type enzyme
M57C
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mutant enzyme shows 40% of the activity of the wild-type enzyme
M85C
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mutant enzyme shows 90% of the activity of the wild-type enzyme
M138C
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mutant enzyme shows 90% of the activity of the wild-type enzyme
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M18C
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mutant enzyme shows 30% of the activity of the wild-type enzyme
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M46C
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mutant enzyme shows 30% of the activity of the wild-type enzyme
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M57C
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mutant enzyme shows 40% of the activity of the wild-type enzyme
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M85C
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mutant enzyme shows 90% of the activity of the wild-type enzyme
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additional information
generation of three catalytically active mutants MaiR-D41/42-304AA, MaiR-D48/49-304AA and MaiR-D52/53-304AA without the hydrophilic and hydrophobic clusters
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
whole cells of Escherichia coli expressing the enzyme mutant MaiR-D48 catalyze the isomerization of maleic acid to fumaric acid at 1 M substrate concentration showing its potential for industrial use
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