Information on EC 2.1.1.80 - protein-glutamate O-methyltransferase

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

EC NUMBER
COMMENTARY
2.1.1.80
-
RECOMMENDED NAME
GeneOntology No.
protein-glutamate O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 2.1.1.24
-
-
formerly
-
glutamate-MTase
-
-
MCP methyltransferase I
-
-
-
-
MCP methyltransferase II
-
-
-
-
methyl-accepting chemotaxis protein methyltransferase II
-
-
-
-
methyl-accepting chemotaxis protein O-methyltransferase
-
-
-
-
methyltransferase CheR
-
-
methyltransferase, protein O-
-
-
-
-
PCMT
-
-
protein carboxyl O-methyltransferase
-
-
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
-
-
-
-
S-adenosylmethionine-glutamyl methyltransferase
-
-
-
-
S-adenosylmethionine:protein-carboxyl O-methyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9055-09-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
MCP methyltransferase I and II
-
-
Manually annotated by BRENDA team
strains S9 and WFS101
-
-
Manually annotated by BRENDA team
occurence of the enzyme in mammalia e.g. bovine and horse is uncertain
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + chemoreceptor carboxyl-terminal pentapeptide NWETF
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + methyl-accepting chemotaxis protein FrzCD-L-glutamate
S-adenosyl-L-homocysteine + methyl-accepting chemotaxis protein FrzCD-L-glutamate methyl ester
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
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
show the reaction diagram
-
membrane chemoreceptor protein
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
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
show the reaction diagram
-
membrane-bound methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
highly specific for S-adenosylmethionine as methyl donor
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
membrane protein involved in chemotaxis
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
specific for the methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
specific for the methyl-accepting chemotaxis proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
membrane chemoreceptor proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [chemotaxis receptor Tar]-L-glutamate
S-adenosyl-L-homocysteine + [chemotaxis receptor Tar]-L-glutamate methyl ester
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the catalytic efficiency of the enzyme increases when Lys3 is present in its di-methylated rather than in its nonmethylated form
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
membrane chemoreceptor proteins
-
?
S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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; Mg2+ and Ca2+ activate MCP methyltransferase II
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+ and Ca2+ activate MCP methyltransferase II
Mg2+
-
Ca2+, Mn2+, Cu2+, Zn2+, Co2+, Fe2+, Fe3+ and Mg2+ at 2 mM have no effect on enzyme activity of methyltransferase I
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
A9145C
-
S-adenosylmethionine analog, antifungal antibiotic
A9145C
-
0.000001 mM, 50% inhibition
Ca2+
-
MCP methyltransferase I
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
-
-
S-adenosyl-L-homocysteine
-
D-isomer is inactive
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
D-isomer is inactive
S-adenosyl-L-homocysteine
-
0.01 mM, 50% inhibition
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
competitive vs. S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
-
Sinefungin
-
S-adenosylmethionine analog, antifungal antibiotic
Sinefungin
-
0.00001 mM, 50% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0077
-
follicle-stimulating hormone
-
-
-
0.046
-
gamma-Globulin
-
-
-
0.1
-
Histone
-
-
0.34
-
Pancreatic ribonuclease
-
-
-
0.00087
-
S-adenosyl-L-methionine
-
thymus enzyme
0.002
-
S-adenosyl-L-methionine
-
MCP methyltransferase I
0.005
-
S-adenosyl-L-methionine
-
-
0.005
-
S-adenosyl-L-methionine
-
MCP methyltransferase II
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0004
-
A1945C
-
-
-
0.000065
-
Ca2+
-
-
0.0002
-
S-adenosyl-L-homocysteine
-
-
0.0009
-
S-adenosyl-L-homocysteine
-
-
0.0026
-
Sinefungin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0000036
-
-
methylation of histone II-A in purine starved cells
0.000076
-
-
-
0.0024
-
-
-
0.0043
-
-
thymus enzyme
0.027
-
-
erythrocyte enzyme
0.03
-
-
brain enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
approx. 30% of maximal activity at pH 6.0, approx. 65% of maximal activity at pH 8.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is mostly expressed in the root endodermis and cortex
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25000
-
-
gel filtration
30000
-
-
gel filtration, SDS-PAGE
32900
-
-
deduced from nucleotide sequence
44000
-
-
MCP methyltransferase I
44000
-
-
gel filtration; MCP methyltransferase I
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 73000, maltose binding protein-tagged enzyme, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 44000, MCP methyltransferase I, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0°C, 0.33 mM dithiothreitol, 0.33 mg/ml bovine serum albumin, 1 week, no loss of activity
-
-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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
maltose binding protein-tagged enzyme is purified by Ni-NTA column chromatography
-
DEAE-Biogel, CM-Biogel, ammonium sulfate, S-adenosylhomocystein affinity column
-
brain enzyme, pH 5.1 treatment, ammonium sulfate, SAH-Sepharose, Sephadex G-100
-
ammonium sulfate, Sephadex G-75, SAH-Sepharose, Sephadex G-75
-
HisTrap HP nickel column chromatography
-
ammonium sulfate, DEAE-cellulose, Phenyl-Sepharose, Bio-gel P-60, hydroxylapatite
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain Tuner
-
expression in Escherichia coli at 30°C under the control of The T7 polymerase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DELTA1-19
-
activity is slightly reduced
K46A
-
moderately reduced activity
R47A
-
mutant protein does not express well, all of the CheR protein is found in inclusion bodies
R53A
-
methyltransferase activity is 4% of the wild-type activity
R56A
-
moderately reduced activity
R57A
-
mutant protein does not express well, all of the CheR protein is found in inclusion bodies
R59A
-
moderately reduced activity