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CheB + H2O
?
-
substrate Cheb is a chemoreceptor
-
-
?
methyl-accepting chemotaxis protein + H2O
chemotaxis protein + methanol
methylated adrenocorticotropic hormone + H2O
adrenocorticotropic hormone
-
-
-
-
?
methylated bovine gamma-globulin + H2O
bovine gamma-globulin + methanol
-
-
-
-
?
methylated calmodulin + H2O
calmodulin + methanol
-
-
-
-
?
methylated deaminated calmodulin + H2O
deaminated calmodulin + methanol
-
-
-
-
?
methylated follicle-stimulating hormone + H2O
follicle-stimulating hormone + methanol
-
-
-
-
?
methylated gelatin + H2O
gelatin + methanol
-
-
-
-
?
methylated growth hormone + H2O
growth hormone + methanol
-
-
-
-
?
methylated histones + H2O
histones + methanol
-
-
-
-
?
methylated luteinizing hormone + H2O
luteinizing hormone + methanol
-
-
-
-
?
methylated methyl-accepting chemotaxis protein + H2O
methyl-accepting chemotaxis protein + methanol
-
-
-
-
?
methylated ovalbumin + H2O
ovalbumin + methanol
-
-
-
-
?
methylated prolactin + H2O
prolactin + methanol
methylated seminal-plasma protein + H2O
seminal-plasma protein + methanol
-
-
-
-
?
methylated seminal-plasma proteins + H2O
seminal-plasma protein + methanol
-
-
-
-
?
ovalbumin methyl ester + H2O
ovalbumin + methanol
-
-
-
-
?
several methylated protein substrates + H2O
?
-
-
-
-
?
additional information
?
-
methyl-accepting chemotaxis protein + H2O
chemotaxis protein + methanol
-
-
-
-
?
methyl-accepting chemotaxis protein + H2O
chemotaxis protein + methanol
-
-
-
-
?
methyl-accepting chemotaxis protein + H2O
chemotaxis protein + methanol
-
-
-
-
?
methylated prolactin + H2O
prolactin + methanol
-
-
-
-
?
methylated prolactin + H2O
prolactin + methanol
-
-
-
-
?
methylated prolactin + H2O
prolactin + methanol
-
-
-
-
?
additional information
?
-
-
cheB mutants show decreased clockwise and counterclockwise event durations and exhibits a significant increase in the flagellar switching frequencies
-
-
?
additional information
?
-
-
enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins
-
-
?
additional information
?
-
-
methylesterae CheB is involved in sensory adaption in bacterial chemotaxis
-
-
?
additional information
?
-
-
the regulation of activity of methylesterase CheB via phosphorylation is central to chemotactic adaption
-
-
?
additional information
?
-
-
the carboxyl-terminal linker is important for chemoreceptor function
-
-
?
additional information
?
-
-
enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins
-
-
?
additional information
?
-
-
in prokaryotes it plays a crucial role in bacterial chemotaxis
-
-
?
additional information
?
-
-
in eukaryotes the enzyme is possibly involved in leukocyte chemotaxis
-
-
?
additional information
?
-
-
enzyme catalyses hydrolysis of receptor glutamine or methylglutamate side-chains to glutamic acid
-
-
?
additional information
?
-
-
responsible for the demethylation of the methyl-accepting chemotaxis proteins
-
-
?
additional information
?
-
-
demethylation of chemotactic membrane receptors
-
-
?
additional information
?
-
-
demethylation of chemotactic membrane receptors
-
-
?
additional information
?
-
-
enzyme catalyses the hydrolysis of glutamyl-methyl esters in bacterial chemoreceptor proteins
-
-
?
additional information
?
-
-
responsible for the demethylation of the methyl-accepting chemotaxis proteins
-
-
?
additional information
?
-
-
surfaces with differing electrostatic properties may reflect CheB regions that mediate protein-protein interaction, computational docking, overview
-
-
?
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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
-
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
-
constructs of the N- and C-terminal domains and investigation of interaction between the isolated regulatory and effector domains of enzyme
additional information
-
constructs of the N- and C-terminal domains and investigation of interaction between the isolated regulatory and effector domains of enzyme
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Kehry, M.R.; Doak, T.G.; Dahlquist, F.W.
Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli
J. Biol. Chem.
259
11828-11835
1984
Escherichia coli
brenda
Gagnon, C.; Harbour, D.; Camato, R.
Purification and characterization of protein methylesterase from rat kidney
J. Biol. Chem.
259
10212-10215
1984
Rattus norvegicus
brenda
Snyder, M.A.; Stock, J.B.; Koshland, D.E.
Carboxylmethyl esterase of bacterial chemotaxis
Methods Enzymol.
106
321-330
1984
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ST89pGK2
brenda
Simms, S.A.; Keane, M.G.; Stock, J.
Multiple forms of the CheB methylesterase in bacterial chemosensing
J. Biol. Chem.
260
10161-10168
1985
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Simms, S.A.; Cornman, E.W.; Mottonen, J.; Stock, J.
Active site of the enzyme which demethylates receptors during bacterial chemotaxis
J. Biol. Chem.
262
29-31
1987
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Krueger, J.K.; Stock, J.; Schutt, C.E.
Evidence that the methylesterase of bacterial chemotaxis may be a serine hydrolase
Biochim. Biophys. Acta
1119
322-326
1992
Escherichia coli, Escherichia coli JM 109
brenda
West, A.H.; Martinez-Hackert, E.; Stock, A.M.
Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB
J. Mol. Biol.
250
276-290
1995
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Anand, G.S.; Goudreau, P.N.; Stock, A.M.
Activation of methylesterase CheB: evidence of a dual role for the regulatory domain
Biochemistry
37
14038-14047
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Goldman, D.J.; Nettleton, D.O.; Ordal, G.W.
Purification and characterization of chemotactic methylesterase from Bacillus subtilis
Biochemistry
23
675-680
1984
Bacillus subtilis
brenda
Veeraragavan, K.; Gagnon, C.
Mammalian protein methylesterase. Physical and enzymic properties
Biochem. J.
260
11-17
1989
Rattus norvegicus
brenda
Veeraragavan, K.; Gagnon, C.
Leupeptin and chymostatin inhibit mammalian protein methylesterase activity
Biochem. Biophys. Res. Commun.
142
603-608
1987
Rattus norvegicus
brenda
Djordjevic, S.; Goudreau, P.N.; Xu, Q.; Stock, A.M.; West, A.H.
Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
Proc. Natl. Acad. Sci. USA
95
1381-1386
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Hughes, C.A.; Mandell, J.G.; Anand, G.S.; Stock, A.M.; Komives, E.A.
Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB
J. Mol. Biol.
307
967-976
2001
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Saxl, R.L.; Anand, G.S.; Stock, A.M.
Synthesis and Biochemical Characterization of a Phosphorylated Analogue of the Response Regulator CheB
Biochemistry
40
12896-12903
2001
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Anand, G.S.; Stock, A.M.
Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB
Biochemistry
41
6752-6760
2002
Salmonella enterica subsp. enterica serovar Typhimurium, Thermotoga maritima
brenda
Lybarger, S.R.; Maddock, J.R.
Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB
J. Bacteriol.
181
5527-5529
1999
Escherichia coli
brenda
Barnakov, A.N.; Barnakova, L.A.; Hazelbauer, G.L.
Location of the receptor-interaction site on CheB, the methylesterase response regulator of bacterial chemotaxis
J. Biol. Chem.
276
32984-32989
2001
Escherichia coli
brenda
Saulmon, M.M.; Karatan, E.; Ordal, G.W.
Effect of loss of CheC and other adaptational proteins on chemotactic behaviour in Bacillus subtilis
Microbiology
150
581-589
2004
Bacillus subtilis
brenda
Bunn, M.W.; Ordal, G.W.
Receptor conformational changes enhance methylesterase activity during chemotaxis by Bacillus subtilis
Mol. Microbiol.
51
721-728
2004
Bacillus subtilis
brenda
Banno, S.; Shiomi, D.; Homma, M.; Kawagishi, I.
Targeting of the chemotaxis methylesterase/deamidase CheB to the polar receptor-kinase cluster in an Escherichia coli cell
Mol. Microbiol.
53
1051-1063
2004
Escherichia coli
brenda
Li, M.; Hazelbauer, G.L.
The carboxyl-terminal linker is important for chemoreceptor function
Mol. Microbiol.
60
469-479
2006
Escherichia coli
brenda
Endres, R.G.; Wingreen, N.S.
Precise adaptation in bacterial chemotaxis through assistance neighborhoods
Proc. Natl. Acad. Sci. USA
103
13040-13044
2006
Escherichia coli (P07330)
brenda
Cho, K.H.; Crane, B.R.; Park, S.
An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain
Biochem. Biophys. Res. Commun.
411
69-75
2011
Thermotoga maritima
brenda