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Protein-glutamate methylesterase

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Protein-glutamate methylesterase

protein-glutamate methylesterase
Identifiers
EC number CAS number IntEnz BRENDA ExPASy KEGG MetaCyc metabolic pathway
PRIAM PDB structures PDBsum
Gene Ontology EGO
CheB_methylest
structural basis for methylesterase cheb regulation by a phosphorylation-activated domain
Identifiers
Symbol CheB_methylest
Pfam InterPro IPR000673
SCOP SUPERFAMILY 1chd

In chemical reaction

protein L-glutamate O5-methyl ester + H2O \rightleftharpoons protein L-glutamate + methanol

Thus, the two substrates of this enzyme are protein L-glutamate O5-methyl ester and H2O, whereas its two products are protein L-glutamate and methanol.

This enzyme is a demethylase, and more specifically it belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is protein-L-glutamate-O5-methyl-ester acylhydrolase. Other names in common use include chemotaxis-specific methylesterase, methyl-accepting chemotaxis protein methyl-esterase, CheB methylesterase, methylesterase CheB, protein methyl-esterase, protein carboxyl methylesterase, PME, protein methylesterase, and protein-L-glutamate-5-O-methyl-ester acylhydrolase. This enzyme participates in 3 metabolic pathways: two-component system - general, bacterial chemotaxis - general, and bacterial chemotaxis - organism-specific.

CheB is part of a two-component signal transduction system. These systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions.[1] Two-component systems are composed of a sensor histidine kinase (HK) and its cognate response regulator (RR).[2] The HK catalyses its own autophosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, in this case a methyltransferase domain.

CheB is involved in chemotaxis. CheB methylesterase is responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). CheB is regulated through phosphorylation by CheA. The N-terminal region of the protein is similar to that of other regulatory components of sensory transduction systems.

Structural studies

As of late 2007, two 1CHD.


References

Further reading

This article incorporates text from the IPR000673


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