Protein-glutamate methylesterase

From Wikipedia, the free encyclopedia

In enzymology, a protein-glutamate methylesterase (EC 3.1.1.61) is an enzyme that catalyzes the 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 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1A2O and 1CHD.

[edit] References

IUBMB entry for 3.1.1.61
BRENDA references for 3.1.1.61 (Recommended.)
PubMed references for 3.1.1.61
PubMed Central references for 3.1.1.61
Google Scholar references for 3.1.1.61
Gagnon C, Harbour D, Camato R (1984). "Purification and characterization of protein methylesterase from rat kidney". J. Biol. Chem. 259: 10212–5. PMID 6469959.
Kehry MR, Doak TG, Dahlquist FW (1984). "Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli". J. Biol. Chem. 259: 11828–35. PMID 6384215.