Protein-glutamate O-methyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a protein-glutamate O-methyltransferase (EC 2.1.1.80) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + protein L-glutamate $\rightleftharpoons$ S-adenosyl-L-homocysteine + protein L-glutamate methyl ester

Thus, the two substrates of this enzyme are S-adenosyl methionine and protein L-glutamic acid, whereas its two products are S-adenosylhomocysteine and protein L-glutamate methyl ester.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:protein-L-glutamate O-methyltransferase. Other names in common use include methyl-accepting chemotaxis protein O-methyltransferase, S-adenosylmethionine-glutamyl methyltransferase, methyl-accepting chemotaxis protein methyltransferase II, S-adenosylmethionine:protein-carboxyl O-methyltransferase, protein methylase II, MCP methyltransferase I, MCP methyltransferase II, protein O-methyltransferase, protein(aspartate)methyltransferase, protein(carboxyl)methyltransferase, protein carboxyl-methylase, protein carboxyl-O-methyltransferase, protein carboxylmethyltransferase II, protein carboxymethylase, protein carboxymethyltransferase, and protein methyltransferase II. This enzyme participates in 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 1AF7 and 1BC5.

[edit] References

IUBMB entry for 2.1.1.80
BRENDA references for 2.1.1.80 (Recommended.)
PubMed references for 2.1.1.80
PubMed Central references for 2.1.1.80
Google Scholar references for 2.1.1.80
Burgess-Cassler A, Ullah AH, Ordal GW (1982). "Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II". J. Biol. Chem. 257: 8412–7. PMID 6806296.
Kleene SJ, Toews ML, Adler J (1977). "Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis". J. Biol. Chem. 252: 3214–8. PMID 16888.
Simms SA, Stock AM, Stock JB (1987). "Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria". J. Biol. Chem. 262: 8537–43. PMID 3298235.
Springer WR, Koshland DE Jr (1977). "Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system". Proc. Natl. Acad. Sci. U. S. A. 74: 533–7. doi:10.1073/pnas.74.2.533. PMID 322131.