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Literature summary extracted from

  • Perez, E.; Zheng, H.; Stock, A.M.
    Identification of methylation sites in Thermotoga maritima chemotaxis receptors (2006), J. Bacteriol., 188, 4093-4100.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.80 S-adenosyl-L-methionine + protein L-glutamate Thermotoga maritima 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-homocysteine + protein L-glutamate methyl ester
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Organism

EC Number Organism UniProt Comment Textmining
2.1.1.80 Thermotoga maritima
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.80 S-adenosyl-L-methionine + protein L-glutamate 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 Thermotoga maritima S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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2.1.1.80 S-adenosyl-L-methionine + protein L-glutamate methylation of specific glutamate residues within the cytoplasmic domains of methyl-accepting chemotaxis proteins: TM0429fl, TM0429c, TM1143fl, TM1143c, TM1428fl, TM1428c Thermotoga maritima S-adenosyl-L-homocysteine + protein L-glutamate methyl ester
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