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J. Biol. Chem., Vol. 262, Issue 18, 8537-8543, 06, 1987
SA Simms, AM Stock and JB Stock
The enzyme (EC 2.1.1.24) from Salmonella typhimurium that catalyzes the
S-adenosylmethionine-dependent methyl esterification of glutamyl residues
in membrane chemoreceptor proteins has been purified to homogeneity, and
the nucleotide sequence of the gene coding for this protein, cheR, has been
determined. The molecular weight, amino acid composition, and N-terminal
amino acid sequence of the purified protein correspond to the values
predicted from the sequence of the gene. The pure protein is a 33-kDa
monomer. Kinetic studies indicate that, at levels of receptor and
S-adenosylmethionine present in wild type cells, the transferase is nearly
saturated. The enzyme has a relatively low turnover number, approximately
10 mol of methylester formed per mol of enzyme per min; and there appear to
be only approximately 200 methyltransferase monomers per wild type cell.
Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria
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