Regulation of methylthioribose kinase by methionine in Klebsiella pneumoniae

P. A. Tower, D. B. Alexander, L. L. Johnson, M. K. Riscoe

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


5-Methylthioribose (MTR) kinase catalyses a key step in the recycling of methionine from 5'-methylthioadenosine, a co-product of polyamine biosynthesis, in Klebsiella pneumoniae. In defined medium lacking methionine, K. pneumoniae exhibits abundant MTR kinase activity. When the bacterium is transferred to a medium containing 10 mM-methionine, the specific activity of MTR kinase decreases in a fashion consistent with repression of new enzyme synthesis and dilution of existing enzyme by cell division. The specific activity of methionine synthase decreases to a similar degree under the same conditions. In Escherichia coli and Salmonella typhimurium, the gene for methionine synthase is co-ordinately controlled as part of the methionine regulon. Taken together, our results indicate that a methionine regulon may function in K. pneumoniae and that expression of MTR kinase may be under its control.

Original languageEnglish (US)
Pages (from-to)1027-1031
Number of pages5
JournalJournal of General Microbiology
Issue number5
StatePublished - 1993
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology


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