EC Number   |
Natural Substrates |
|---|
   2.1.1.80 | S-adenosyl-L-methionine + chemotaxis receptors McpS L-glutamate |
substrate for isoform CheR2 only |
| 2.1.1.80 | S-adenosyl-L-methionine + chemotaxis receptors McpT L-glutamate |
substrate for isoform CheR2 only |
| 2.1.1.80 | S-adenosyl-L-methionine + methyl-accepting chemotaxis protein B L-glutamate |
exklusive substrate of CheR2 |
| 2.1.1.80 | S-adenosyl-L-methionine + protein L-glutamate |
- |
| 2.1.1.80 | S-adenosyl-L-methionine + protein L-glutamate |
membrane chemoreceptor proteins |
| 2.1.1.80 | S-adenosyl-L-methionine + protein L-glutamate |
enzyme is essential for maintaining the appropriate rate constants and levels of the regulator of the chemotactic response |
| 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 |
| 2.1.1.80 | S-adenosyl-L-methionine + protein L-glutamate |
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 |
| 2.1.1.80 | 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 |
