Information on EC 3.1.1.61 - protein-glutamate methylesterase

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

EC NUMBER
COMMENTARY hide
3.1.1.61
-
RECOMMENDED NAME
GeneOntology No.
protein-glutamate methylesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-L-glutamate-O5-methyl-ester acylhydrolase
Hydrolyses the products of EC 2.1.1.77 (protein-L-isoaspartate(D-aspartate) O-methyltransferase), EC 2.1.1.78 (isoorientin 3'-O-methyltransferase), EC 2.1.1.80 (protein-glutamate O-methyltransferase) and EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
69552-31-4
-
93792-01-9
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
interaction mode between CheB and chemoreceptors, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CheB + H2O
?
show the reaction diagram
-
substrate Cheb is a chemoreceptor
-
-
?
methyl-accepting chemotaxis protein + H2O
chemotaxis protein + methanol
show the reaction diagram
methylated adrenocorticotropic hormone + H2O
adrenocorticotropic hormone
show the reaction diagram
-
-
-
-
?
methylated bovine gamma-globulin + H2O
bovine gamma-globulin + methanol
show the reaction diagram
-
-
-
-
?
methylated calmodulin + H2O
calmodulin + methanol
show the reaction diagram
-
-
-
-
?
methylated follicle-stimulating hormone + H2O
follicle-stimulating hormone + methanol
show the reaction diagram
-
-
-
-
?
methylated gelatin + H2O
gelatin + methanol
show the reaction diagram
-
-
-
-
?
methylated growth hormone + H2O
growth hormone + methanol
show the reaction diagram
-
-
-
-
?
methylated histones + H2O
histones + methanol
show the reaction diagram
-
-
-
-
?
methylated luteinizing hormone + H2O
luteinizing hormone + methanol
show the reaction diagram
-
-
-
-
?
methylated prolactin + H2O
prolactin + methanol
show the reaction diagram
-
-
-
-
?
methylated seminal-plasma proteins + H2O
seminal-plasma protein + methanol
show the reaction diagram
-
-
-
-
?
ovalbumin methyl ester + H2O
ovalbumin + methanol
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
CheB + H2O
?
show the reaction diagram
-
substrate Cheb is a chemoreceptor
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
as effective as Mg2+ in activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chymostatin
-
-
D-Phe-Pro-Arg-H
-
-
Divalent ions
-
-
-
Leupeptin
-
-
N-tert-Butoxycarbonyl-Gln-Leu-Lys-H
-
-
P2 domain of histidine kinase
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inhibition is decreased upon phosphorylation
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Pepstatin
-
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
deaminated calmodulin
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pH 6.0, 37C
-
0.015
methyl-accepting chemotaxis protein
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pH 7.0, 30C
-
0.0026
methylated adrenocorticotropic hormone
-
pH 6.0, 37C
-
0.063
methylated bovine gamma-globulin
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pH 6.0, 37C
-
0.0009
methylated calmodulin
-
pH 6.0, 37C
-
0.0024
methylated follicle-stimulating hormone
-
pH 6.0, 37C
-
0.0013
methylated gelatin
-
pH 6.0, 37C
-
0.0174
methylated growth hormone
-
pH 6.0, 37C
-
0.0005
methylated histone
-
pH 6.0, 37C
0.0019
methylated luteinizing hormone
-
pH 6.0, 37C
-
0.00001
methylated methyl-accepting chemotaxis protein
-
pH 7.0, 22C
-
0.0072
methylated ovalbumin
-
pH 6.0, 37C
-
0.026
methylated prolactin
-
pH 7.0, 30C
-
0.0021
methylated seminal-plasma protein
-
pH 6.0, 37C
-
0.0059
ovalbumin methyl ester
-
pH 6.0, 37C
-
additional information
additional information
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-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
methyl-accepting chemotaxis protein
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
0.00002 - 0.00056
several methylated protein substrates
Rattus norvegicus
-
-
-
additional information
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
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-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00054
chymostatin
-
pH 6.0, 37C
0.000035
Leupeptin
-
pH 6.0, 37C
0.0025 - 0.021
P2 domain of histidine kinase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
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50% of activity maximum at 20C and 37C, about 60% of activity maximum at 22C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from caput epididymidis, level declines more than 20fold during maturation as spermatozoa acquire motility and capacity to fertilize
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
CheB localizes to a cell pole in presence of the chemoreceptor MCP, binding of the NL domain to the P2 domain targets methylesterase CheB to the polar signalling complex
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
gel filtration
41000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the catalytic domain
-
the crystal structure model suggests a structural basis for phosphorylation-dependent activation of effector function
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CheB methylesterase domain, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 10
-
30 min, stable
646046
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
maximal stability and low activity is observed in phosphate buffer at pH 7 with 50-100 mM added NaCl, while MES and low salt concentration afford minimum protection against inactivation
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stabilized by aqueous glycerol solution
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM sodium acetate buffer, pH 4.35, 50% glycerol, 0.1 mM DTT, purified enzyme stable
-
-70C, stable for at least 1 month
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4C, 10% glycerol, 0.04% sodium azide, stable for at least several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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strain ST89pGK2, plasmid bearing strain overproducing esterase and transferase
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D54N
-
mutation of aspartate phosphorylation site causes no loss of activity, provided the enzyme is sufficiently induced
DELTA1-140
-
truncated enzyme form is active
S173C
-
no release of methanol, even when induced
C207A
-
mutant retains at least 50% of the wild-type enzyme activity
C207A/C309A
-
the double mutant retains at 70% of the wild-type enzyme activity
C309A
-
mutant retains at least 50% of the wild-type enzyme activity
S164C
-
mutant has less than 2% of the wild-type activity
C207A
-
mutant retains at least 50% of the wild-type enzyme activity
-
C207A/C309A
-
the double mutant retains at 70% of the wild-type enzyme activity
-
C309A
-
mutant retains at least 50% of the wild-type enzyme activity
-
S164C
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mutant has less than 2% of the wild-type activity
-
A137T
-
3fold higher enzyme activity than wild-type enzyme in absence of phosphoramidate, in presence of phosphoramidate mutant and wild-type proteins show similar increase in enzyme activity
C207A
-
mutation has no effect on enzyme activity
C207S/C309S
-
wild-type and mutant enzyme show significantly greater activity than the unphosphorylated proteins
C309A
-
mutation causes a complete loss of enzyme activity
D56C/C207S/C309S
-
the half-life of mutant-SPO3 is 28 days, the unphosphorylated wild-type and mutant enzyme show the same enzyme activities
D56N
-
no activation of enzyme activity in the presence of phosphoramidate
G84V
-
mutation causes a complete loss of enzyme activity
H138R
-
2.5fold higher enzyme activity than wild-type enzyme in absence of phosphoramidate, in presence of phosphoramidate mutant and wild-type proteins show similar increase in enzyme activity
L153P
-
2fold higher enzyme activity than wild-type enzyme in absence of phosphoramidate, in presence of phosphoramidate mutant and wild-type proteins show similar increase in enzyme activity
R255W
-
4fold higher enzyme activity than wild-type enzyme in absence of phosphoramidate, in presence of phosphoramidate mutant and wild-type proteins show similar increase in enzyme activity
additional information
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