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Literature summary for 2.1.1.80 extracted from

  • Lai, W.C.; Hazelbauer, G.L.
    Carboxyl-terminal extensions beyond the conserved pentapeptide reduce rates of chemoreceptor adaptational modification (2005), J. Bacteriol., 187, 5115-5121.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + protein L-glutamate Escherichia coli 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-homocysteine + protein L-glutamate methyl ester
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + protein L-glutamate
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Escherichia coli S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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S-adenosyl-L-methionine + protein L-glutamate 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 Escherichia coli S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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Synonyms

Synonyms Comment Organism
methyltransferase CheR
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Escherichia coli