Purification and characterization of the S-adenosylmethionine: glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria.

S. A. Simms, A. M. Stock, J. B. Stock

Research output: Contribution to journalArticle

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)8537-8543
Number of pages7
JournalJournal of Biological Chemistry
Volume262
Issue number18
StatePublished - Jun 25 1987

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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