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Information on EC 2.1.1.80 - protein-glutamate O-methyltransferase
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EC Tree
2.1.1.80 protein-glutamate O-methyltransferaseIUBMB Comments
Forms ester groups with L-glutamate residues in a number of membrane proteins.
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Word Map
- 2.1.1.80
- methyltransferases
-
2.1.1.24
-
chemoreceptor
- cheb
-
methylesterase
- s-adenosyl-l-homocysteine
-
l-isoaspartyl
-
d-aspartyl
- sinefungin
- l-isoaspartate
-
methyl-acceptor
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
protein methyltransferase, protein methylase ii, cher1, methyltransferase cher, cher2, protein carboxymethylase, protein carboxymethyltransferase, protein carboxyl-methylase, protein o-methyltransferase, omtf3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CheR
CheR1
CheR2
CheR3
EC 2.1.1.24
-
-
formerly
-
MCP methyltransferase I
-
-
-
-
MCP methyltransferase II
-
-
-
-
methyl-accepting chemotaxis protein methyltransferase II
-
-
-
-
methyl-accepting chemotaxis protein O-methyltransferase
-
-
-
-
methyltransferase, protein O-
-
-
-
-
protein carboxyl-methylase
-
-
-
-
protein carboxyl-O-methyltransferase
-
-
-
-
protein carboxylmethyltransferase II
-
-
-
-
protein carboxymethylase
-
-
-
-
protein carboxymethyltransferase
-
-
-
-
protein methylase II
-
-
-
-
protein methyltransferase II
-
-
-
-
protein O-methyltransferase
-
-
-
-
protein(aspartate)methyltransferase
-
-
-
-
protein(carboxyl)methyltransferase
-
-
-
-
R0248
S-adenosylmethionine-glutamyl methyltransferase
-
-
-
-
S-adenosylmethionine:protein-carboxyl O-methyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
random mechanism with no abortive complexes being formed, sequential random bi bi mechanism
-
S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase
Forms ester groups with L-glutamate residues in a number of membrane proteins.
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CAS REGISTRY NUMBER
COMMENTARY
9055-09-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + chemoreceptor carboxyl-terminal pentapeptide NWETF
?
-
-
-
-
?
S-adenosyl-L-methionine + chemoreceptor Tar L-glutamate
S-adenosyl-L-homocysteine + chemoreceptor Tar L-glutamate methyl ester
-
chemoreceptor Tar bearing the carboxylterminal pentapeptide NWETF
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpS L-glutamate methyl ester
S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpT L-glutamate methyl ester
S-adenosyl-L-methionine + methyl-accepting chemotaxis protein B L-glutamate
S-adenosyl-L-homocysteine + methyl-accepting chemotaxis protein B L-glutamate methyl ester
exklusive substrate of CheR2
-
-
?
S-adenosyl-L-methionine + methyl-accepting chemotaxis protein FrzCD-L-glutamate
S-adenosyl-L-homocysteine + methyl-accepting chemotaxis protein FrzCD-L-glutamate methyl ester
-
full-length FrzF methylates FrzCD on a single residue, E182, while FrzF lacking tetra trico-peptide repeats methylates FrzCD on three residues, E168, E175, and E182
-
-
?
S-adenosyl-L-methionine + PIP2;1 peptide
?
-
the enzyme acts on the N-terminal tail of aquaporin PIP2;1 at Glu6 and is able to methylate both the un- and dimethylated peptide forms
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
S-adenosyl-L-methionine + [chemotaxis receptor Tar]-L-glutamate
S-adenosyl-L-homocysteine + [chemotaxis receptor Tar]-L-glutamate methyl ester
S-adenosyl-L-methionine + [follicle-stimulating hormone]-L-glutamate
S-adenosyl-L-homocysteine + [follicle-stimulating hormone]-L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + [gamma-globulin]-L-glutamate
S-adenosyl-L-homocysteine + [gamma-globulin]-L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + [histone]-L-glutamate
S-adenosyl-L-homocysteine + [histone]-L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + [pancreatic ribonuclease]-L-glutamate
S-adenosyl-L-homocysteine + [pancreatic ribonuclease]-L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + [protein]-L-glutamate
S-adenosyl-L-homocysteine + [protein]-L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpS L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpS L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpT L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpT L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
methyltransferase I is unable to methylate E. coli membranes
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane-bound methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
S-adenosyl-L-ethionine shows 2.4% donor efficiency compared to S-adenosyl-L-methionine
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
highly specific for S-adenosylmethionine as methyl donor
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
S-adenosyl-L-ethionine shows 2.4% donor efficiency compared to S-adenosyl-L-methionine
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
highly specific for S-adenosylmethionine as methyl donor
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
specific for the methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
specific for the methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
sensory adaptation in bacterial chemotaxis is mediated by covalent modification of chemoreceptors. Specific glutamyl residues are methylated and demethylated in reactions catalyzed by methyltransferase CheR and methylesterase CheB. Efficient modification by either enzyme is dependent on a conserved pentapeptide sequence, NWETF or NWESF, present at the extreme carboxyl terminus of high-abundance chemoreceptors. Maximal enhancement of the reactions of adaptational modification by the pentapeptide NWETF requires that this sequence is the final residues at the carboxyl terminus of a chemoreceptor. Receptors with carboxyl-terminal extensions past the pentapeptide exhibited rates of modification lower than a wild-type receptor but higher than the low rates for receptors deleted of the pentapeptide. The effect is greater for CheB-catalyzed modifications than for CheR-catalyzed methylation
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
enzyme does not catalyze the methylation of a variety of soluble proteins, including ovalbumin, ribonuclease and lysozyme
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane chemoreceptor protein
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
specific for proteins in Salmonella typhimurium and E. coli membranes
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
S-adenosyl-L-ethionine shows 2.4% donor efficiency compared to S-adenosyl-L-methionine
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
highly specific for S-adenosylmethionine as methyl donor
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
specific for the methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane chemoreceptor proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
enzyme is essential for maintaining the appropriate rate constants and levels of the regulator of the chemotactic response
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
anti-bovine serum albumin antibody can be carboxylmethylated via spleen PCMT to a level similar to gamma-globulinglobulin. This carboxylmethylation increased the hydrophobicity of the anti-bovine serum albumin antibody up to 11.4%, and enhances the antigen-binding activity of this antibody up to 24.6%. Protein carboxylmethylation may reversibly regulate the antibody-mediated immunological events via the Fc region
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
anti-bovine serum albumin antibody can be carboxylmethylated via spleen PCMT to a level similar to gamma-globulinglobulin. This carboxylmethylation increases the hydrophobicity of the anti-bovine serum albumin antibody up to 11.4%, and enhances the antigen-binding activity of this antibody up to 24.6%
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
adaptation in bacterial chemotaxis involves reversible methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins. Fifteen sites of methylation are identified within the cytoplasmic domains of four different chemoreceptors. The results establish a consensus sequence for chemoreceptor methylation sites in Thermotoga maritima that is distinct from the previously identified consensus sequence
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins: TM0429fl, TM0429c, TM1143fl, TM1143c, TM1428fl, TM1428c
-
-
?
S-adenosyl-L-methionine + [chemotaxis receptor Tar]-L-glutamate
S-adenosyl-L-homocysteine + [chemotaxis receptor Tar]-L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + [chemotaxis receptor Tar]-L-glutamate
S-adenosyl-L-homocysteine + [chemotaxis receptor Tar]-L-glutamate methyl ester
-
-
-
-
?
additional information
?
-
-
the catalytic efficiency of the enzyme increases when Lys3 is present in its di-methylated rather than in its nonmethylated form
-
-
?
additional information
?
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
additional information
?
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
additional information
?
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
additional information
?
-
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
additional information
?
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
additional information
?
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
additional information
?
-
no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpS L-glutamate methyl ester
S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpT L-glutamate methyl ester
S-adenosyl-L-methionine + methyl-accepting chemotaxis protein B L-glutamate
S-adenosyl-L-homocysteine + methyl-accepting chemotaxis protein B L-glutamate methyl ester
exklusive substrate of CheR2
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpS L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpS L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpT L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate
S-adenosyl-L-homocysteine + chemotaxis receptors McpT L-glutamate methyl ester
substrate for isoform CheR2 only
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
sensory adaptation in bacterial chemotaxis is mediated by covalent modification of chemoreceptors. Specific glutamyl residues are methylated and demethylated in reactions catalyzed by methyltransferase CheR and methylesterase CheB. Efficient modification by either enzyme is dependent on a conserved pentapeptide sequence, NWETF or NWESF, present at the extreme carboxyl terminus of high-abundance chemoreceptors. Maximal enhancement of the reactions of adaptational modification by the pentapeptide NWETF requires that this sequence is the final residues at the carboxyl terminus of a chemoreceptor. Receptors with carboxyl-terminal extensions past the pentapeptide exhibited rates of modification lower than a wild-type receptor but higher than the low rates for receptors deleted of the pentapeptide. The effect is greater for CheB-catalyzed modifications than for CheR-catalyzed methylation
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
membrane chemoreceptor proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
enzyme is essential for maintaining the appropriate rate constants and levels of the regulator of the chemotactic response
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
anti-bovine serum albumin antibody can be carboxylmethylated via spleen PCMT to a level similar to gamma-globulinglobulin. This carboxylmethylation increased the hydrophobicity of the anti-bovine serum albumin antibody up to 11.4%, and enhances the antigen-binding activity of this antibody up to 24.6%. Protein carboxylmethylation may reversibly regulate the antibody-mediated immunological events via the Fc region
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
-
adaptation in bacterial chemotaxis involves reversible methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins. Fifteen sites of methylation are identified within the cytoplasmic domains of four different chemoreceptors. The results establish a consensus sequence for chemoreceptor methylation sites in Thermotoga maritima that is distinct from the previously identified consensus sequence
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
-
activates, Ca2+ is somewhat more effective than Mg2+, optimum: 5 mM Ca2+
Ca2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
Ca2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
Ca2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
Mg2+
-
activates, Ca2+ is somewhat more effective than Mg2+, optimum: 5 mM Ca2+
Mg2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
Mg2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
Mg2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
0.4 mM, 40% inhibition, can be reversed by 12 mM 2-mercaptoethanol
S-adenosyl-L-homocysteine
-
D-isomer is inactive
S-adenosyl-L-homocysteine
-
competitive vs. S-adenosyl-L-methionine
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Prognostic value of HER2 status on circulating tumor cells in advanced-stage breast cancer patients with HER2-negative tumors.
Carcinoma
Characterization of the Enzymatic Activity of SETDB1 and Its 1:1 Complex with ATF7IP.
Carcinoma
Evolutionary Expression of HER2 Conferred by Chromosome Aneuploidy on Circulating Gastric Cancer Cells Contributes to Developing Targeted and Chemotherapeutic Resistance.
Carcinoma, Hepatocellular
PRMT6 Regulates RAS/RAF Binding and MEK/ERK-Mediated Cancer Stemness Activities in Hepatocellular Carcinoma through CRAF Methylation.
Cholestasis
Lobe-specific heterogeneity in asymmetric dimethylarginine and matrix metalloproteinase levels in a rat model of obstructive cholestasis.
Choline Deficiency
The effects of ethionine administration and choline deficiency on protein carboxymethylase activity in mouse pancreas.
Diabetes Insipidus
High-protein carboxymethylase activity and low endogenous methyl acceptor proteins in posterior pituitary lobe of rats lacking neurophysin-vasopressin (Brattleboro rats).
Leukemia
DOT1L inhibitor EPZ-5676 displays synergistic antiproliferative activity in combination with standard of care drugs and hypomethylating agents in MLL-rearranged leukemia cells.
Leukemia
Mechanisms of Pinometostat (EPZ-5676) Treatment-Emergent Resistance in MLL-Rearranged Leukemia.
Lymphoma
EPZ011989, A Potent, Orally-Available EZH2 Inhibitor with Robust in Vivo Activity.
Melanoma
Characterization of the Enzymatic Activity of SETDB1 and Its 1:1 Complex with ATF7IP.
Neoplasms
A concordant expression pattern of fatty acid synthase and membranous human epidermal growth factor receptor 2 exists in gastric cancer and is associated with a poor prognosis in gastric adenocarcinoma patients.
Neoplasms
Biological processes and signal transduction pathways regulated by the protein methyltransferase SETD7 and their significance in cancer.
Neoplasms
Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors.
Neoplasms
Development of novel SUV39H2 inhibitors that exhibit growth suppressive effects in mouse xenograft models and regulate the phosphorylation of H2AX.
Neoplasms
EPZ011989, A Potent, Orally-Available EZH2 Inhibitor with Robust in Vivo Activity.
Neoplasms
In Situ Proteome Profiling and Bioimaging Applications of Small-Molecule Affinity-Based Probes Derived From DOT1L Inhibitors.
Neoplasms
Mimicking H3 Substrate Arginine in the Design of G9a Lysine Methyltransferase Inhibitors for Cancer Therapy: A Computational Study for Structure-Based Drug Design.
Neoplasms
PRMT6 Regulates RAS/RAF Binding and MEK/ERK-Mediated Cancer Stemness Activities in Hepatocellular Carcinoma through CRAF Methylation.
Neoplasms
Prognostic value of HER2 status on circulating tumor cells in advanced-stage breast cancer patients with HER2-negative tumors.
Neoplasms
Protein methyltransferase inhibitors as precision cancer therapeutics: a decade of discovery.
Neoplasms
RIZ1 is epigenetically inactivated by promoter hypermethylation in thyroid carcinoma.
Neoplasms
Smyd3 Is a Transcriptional Potentiator of Multiple Cancer-Promoting Genes and Required for Liver and Colon Cancer Development.
Neuroblastoma
Characterization of protein carboxyl-O-methyltransferase in the spontaneous in vivo murine C-1300 neuroblastoma.
Neuroblastoma
Protein carboxyl-O-methyltransferase activity in cultured C-1300 neuroblastoma cells.
Retinoblastoma
Altered expression of retinoblastoma protein-interacting zinc finger gene, RIZ, in human leukaemia.
Retinoblastoma
Modulation of RIZ gene expression is associated to estradiol control of MCF-7 breast cancer cell proliferation.
Sarcoma, Avian
Selective methylation of rous sarcoma virus glycoproteins by protein methylase II.
Subacute Combined Degeneration
Correlation between inhibition of myelin basic protein (arginine) methyltransferase by sinefungin and lack of compact myelin formation in cultures of cerebral cells from embryonic mice.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
S-adenosyl-L-methionine
-
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
approx. 30% of maximal activity at pH 6.0, approx. 65% of maximal activity at pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is mostly expressed in the root endodermis and cortex
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
enzyme gene disruption results in loss of motility and significantly impairs symbiotic competency with the liverwort Blasia pusilla
malfunction
-
enzyme gene disruption results in loss of motility and significantly impairs symbiotic competency with the liverwort Blasia pusilla
-
metabolism
-
the enzyme catalyzes the methylation of the cytosolic domain of the membrane-bound chemotaxis receptors, and plays a pivotal role in the chemotactic signal transduction pathway
metabolism
-
the enzyme catalyzes methylation of specific glutamate residues in the cytoplasmic domain of methyl-accepting chemotactic protein receptors which is essential for the chemical sensing and chemotactic bacterial mobility towards favorable chemicals or away from unfavorable ones
physiological function
isoform CheR1 is required for efficient biofilm formation
physiological function
isoform CheR2 is essential for chemotaxis
physiological function
-
isoform CheR1 is required for efficient biofilm formation
-
Show AA Sequence and Transmembrane Helices (28869 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32247
1 * 32247, isoform CheR2, calculated from amino acid sequence
32900
-
deduced from nucleotide sequence
38600
1 * 38600, isoform CheR2, sedimentation equilibrium ultracentrifugation
44000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 32247, isoform CheR2, calculated from amino acid sequence
monomer
1 * 38600, isoform CheR2, sedimentation equilibrium ultracentrifugation
monomer
-
1 * 32247, isoform CheR2, calculated from amino acid sequence
-
monomer
-
1 * 38600, isoform CheR2, sedimentation equilibrium ultracentrifugation
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R47A
-
mutant protein does not express well, all of the CheR protein is found in inclusion bodies
R57A
-
mutant protein does not express well, all of the CheR protein is found in inclusion bodies
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20-50% glycerol, 5 mM sodium borate, 5 mM EDTA, 2.4 mM 2-mercaptoethanol, pH 9.3, 1 year, no loss of activity
-
0°C, 0.33 mM dithiothreitol, 0.33 mg/ml bovine serum albumin, 1 week, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-cellulose, Phenyl-Sepharose, Bio-gel P-60, hydroxylapatite
-
DEAE-Biogel, CM-Biogel, ammonium sulfate, S-adenosylhomocystein affinity column
-
maltose binding protein-tagged enzyme is purified by Ni-NTA column chromatography
-
Ni-NTA column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli at 30°C under the control of The T7 polymerase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Simms, S.A.; Stock, A.M.; Stock, J.B.
Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria
J. Biol. Chem.
262
8537-8543
1987
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Springer, W.R.; Koshland, D.E.
Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system
Proc. Natl. Acad. Sci. USA
74
533-537
1977
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Burgess-Cassler, A.; Ullah, A.H.J.; Ordal, G.W.
Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II
J. Biol. Chem.
257
8412-8417
1982
Bacillus subtilis
brenda
Kleene, S.J.; Toews, M.L.; Adler, J.
Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis
J. Biol. Chem.
252
3214-3218
1977
Escherichia coli
brenda
Stock, J.B.; Clarke, S.; Koshland, D.E.
The protein carboxylmethyltransferase involved in Escherichia coli and Salmonella typhimurium chemotaxis
Methods Enzymol.
106
310-321
1984
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kim, S.
S-Adenosylmethionine: protein-carboxyl O-methyltransferase (protein methylase II)
Methods Enzymol.
106
295-309
1984
Bacillus subtilis, Bos taurus, Escherichia coli, Homo sapiens, Mammalia, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Rollins, C.M.; Dahlquist, F.W.
Methylation of chemotaxis-specific proteins in Escherichia coli cells permeable to S-adenosylmethionine
Biochemistry
19
4627-4632
1980
Escherichia coli
brenda
Clarke, S.
Protein carboxyl methyltransferases: two distinct classes of enzymes
Annu. Rev. Biochem.
54
479-506
1985
Bacillus subtilis, Escherichia coli, Mammalia, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ullah, A.H.J.; Ordal, G.W.
Purification and characterization of methyl-accepting chemotaxis protein methyltransferase I in Bacillus subtilis
Biochem. J.
199
795-805
1981
Bacillus subtilis
brenda
Simms, S.A.; Subbaramaiah, K.
The kinetic mechanism of S-adenosyl-L-methionine: glutamylmethyltransferase from Salmonella typhimurium
J. Biol. Chem.
266
12741-12746
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Alleman, M.M.; Mann, V.H.; Bacchi, C.J.; Yarlett, N.; Gottlieb, M.; Dwyer, D.M.
Crithidia luciliae: effect of purine starvation on S-adenosyl-L-methionine uptake and protein methylation
Exp. Parasitol.
81
519-528
1995
Crithidia luciliae
brenda
Perez, E.; West, A.H.; Stock, A.M.; Djordjevic, S.
Discrimination between different methylation states of chemotaxis receptor Tar by receptor methyltransferase CheR
Biochemistry
43
953-961
2004
Salmonella enterica
brenda
Park, J.S.; Cho, J.Y.; Kim, S.S.; Bae, H.J.; Han, J.W.; Lee, H.W.; Hong, S.Y.
Immunoglobulin can be functionally regulated by protein carboxylmethylation in Fc region
Arch. Pharm. Res.
29
384-393
2006
Sus scrofa
brenda
Lai, W.C.; Hazelbauer, G.L.
Carboxyl-terminal extensions beyond the conserved pentapeptide reduce rates of chemoreceptor adaptational modification
J. Bacteriol.
187
5115-5121
2005
Escherichia coli
brenda
Perez, E.; Zheng, H.; Stock, A.M.
Identification of methylation sites in Thermotoga maritima chemotaxis receptors
J. Bacteriol.
188
4093-4100
2006
Thermotoga maritima
brenda
Koch, M.K.; Staudinger, W.F.; Siedler, F.; Oesterhelt, D.
Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum
J. Mol. Biol.
380
285-302
2008
Halobacterium salinarum
brenda
Scott, A.E.; Simon, E.; Park, S.K.; Andrews, P.; Zusman, D.R.
Site-specific receptor methylation of FrzCD in Myxococcus xanthus is controlled by a tetra-trico peptide repeat (TPR) containing regulatory domain of the FrzF methyltransferase
Mol. Microbiol.
69
724-735
2008
Myxococcus xanthus
brenda
Muppirala, U.K.; Desensi, S.; Lybrand, T.P.; Hazelbauer, G.L.; Li, Z.
Molecular modeling of flexible arm-mediated interactions between bacterial chemoreceptors and their modification enzyme
Protein Sci.
18
1702-1714
2009
Escherichia coli
brenda
Sahr, T.; Adam, T.; Fizames, C.; Maurel, C.; Santoni, V.
O-carboxyl- and N-methyltransferases active on plant aquaporins
Plant Cell Physiol.
51
2092-2104
2010
Arabidopsis thaliana
brenda
Batra, M.; Sharma, R.; Chandra, V.; Aggarwal, M.; Agarwal, U.; Gupta, P.; Singh, R.P.; Tomar, S.
In silico and proteomic analysis of protein methyltransferase CheR from Bacillus subtilis
Int. J. Biol. Macromol.
77
168-180
2015
Bacillus subtilis
brenda
Garcia-Fontana, C.; Reyes-Darias, J.A.; Munoz-Martinez, F.; Alfonso, C.; Morel, B.; Ramos, J.L.; Krell, T.
High specificity in CheR methyltransferase function: CheR2 of Pseudomonas putida is essential for chemotaxis, whereas CheR1 is involved in biofilm formation
J. Biol. Chem.
288
18987-18999
2013
Pseudomonas putida (Q88ER1), Pseudomonas putida (Q88GG4), Pseudomonas putida (Q88MS8), Pseudomonas putida, Pseudomonas putida KT 2240 (Q88ER1), Pseudomonas putida KT 2240 (Q88GG4), Pseudomonas putida KT 2240 (Q88MS8)
brenda
Garcia-Fontana, C.; Lugo, A.; Krell, T.
Structural biology: Specificity of the CheR2 methyltransferase in Pseudomonas aeruginosa is directed by a C-terminal pentapeptide in the McpB chemoreceptor
Sci. Signal.
7
ra34
2014
Pseudomonas aeruginosa (Q9I6V7), Pseudomonas aeruginosa
brenda
Duggan, P.; Thiel, T.; Adams, D.
Symbiosis between the cyanobacterium Nostoc and the liverwort Blasia requires a CheR-type MCP methyltransferase
Symbiosis
59
111-120
2013
Nostoc punctiforme (B2J4R2), Nostoc punctiforme ATCC 29133 (B2J4R2)
-
brenda
Batra, M.; Sharma, R.; Malik, A.; Dhindwal, S.; Kumar, P.; Tomar, S.
Crystal structure of pentapeptide-independent chemotaxis receptor methyltransferase (CheR) reveals idiosyncratic structural determinants for receptor recognition
J. Struct. Biol.
196
364-374
2016
Bacillus subtilis
brenda
Li, M.; Hazelbauer, G.L.
Methyltransferase CheR binds to its chemoreceptor substrates independent of their signaling conformation yet modifies them differentially
Protein Sci.
29
443-454
2020
Escherichia coli
brenda
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