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S-adenosyl-L-methionine + chemoreceptor carboxyl-terminal pentapeptide NWETF
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S-adenosyl-L-methionine + chemoreceptor Tar L-glutamate
S-adenosyl-L-homocysteine + chemoreceptor Tar L-glutamate methyl ester
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chemoreceptor Tar bearing the carboxylterminal pentapeptide NWETF
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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
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S-adenosyl-L-methionine + methyl-accepting chemotaxis protein FrzCD-L-glutamate
S-adenosyl-L-homocysteine + methyl-accepting chemotaxis protein FrzCD-L-glutamate methyl ester
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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
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S-adenosyl-L-methionine + PIP2;1 peptide
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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
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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
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S-adenosyl-L-methionine + [gamma-globulin]-L-glutamate
S-adenosyl-L-homocysteine + [gamma-globulin]-L-glutamate methyl ester
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S-adenosyl-L-methionine + [histone]-L-glutamate
S-adenosyl-L-homocysteine + [histone]-L-glutamate methyl ester
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S-adenosyl-L-methionine + [pancreatic ribonuclease]-L-glutamate
S-adenosyl-L-homocysteine + [pancreatic ribonuclease]-L-glutamate methyl ester
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S-adenosyl-L-methionine + [protein]-L-glutamate
S-adenosyl-L-homocysteine + [protein]-L-glutamate methyl ester
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additional information
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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
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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
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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
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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
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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methyltransferase I is unable to methylate E. coli membranes
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane-bound methyl-accepting chemotaxis proteins
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-ethionine shows 2.4% donor efficiency compared to S-adenosyl-L-methionine
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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highly specific for S-adenosylmethionine as methyl donor
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane protein involved in chemotaxis
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane protein involved in chemotaxis
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-ethionine shows 2.4% donor efficiency compared to S-adenosyl-L-methionine
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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highly specific for S-adenosylmethionine as methyl donor
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane protein involved in chemotaxis
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane protein involved in chemotaxis
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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specific for the methyl-accepting chemotaxis proteins
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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specific for the methyl-accepting chemotaxis proteins
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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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
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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enzyme does not catalyze the methylation of a variety of soluble proteins, including ovalbumin, ribonuclease and lysozyme
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane chemoreceptor protein
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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specific for proteins in Salmonella typhimurium and E. coli membranes
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-ethionine shows 2.4% donor efficiency compared to S-adenosyl-L-methionine
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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highly specific for S-adenosylmethionine as methyl donor
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane protein involved in chemotaxis
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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specific for the methyl-accepting chemotaxis proteins
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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membrane chemoreceptor proteins
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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enzyme is essential for maintaining the appropriate rate constants and levels of the regulator of the chemotactic response
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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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
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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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%
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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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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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S-adenosyl-L-methionine + protein L-glutamate
S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins: TM0429fl, TM0429c, TM1143fl, TM1143c, TM1428fl, TM1428c
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S-adenosyl-L-methionine + [chemotaxis receptor Tar]-L-glutamate
S-adenosyl-L-homocysteine + [chemotaxis receptor Tar]-L-glutamate methyl ester
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S-adenosyl-L-methionine + [chemotaxis receptor Tar]-L-glutamate
S-adenosyl-L-homocysteine + [chemotaxis receptor Tar]-L-glutamate methyl ester
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additional information
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the catalytic efficiency of the enzyme increases when Lys3 is present in its di-methylated rather than in its nonmethylated form
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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additional information
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no activity with chemotaxis receptors McpS and chemotaxis receptors McpT
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