Abstract
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 language | English (US) |
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Pages (from-to) | 1027-1031 |
Number of pages | 5 |
Journal | Journal of General Microbiology |
Volume | 139 |
Issue number | 5 |
DOIs | |
State | Published - 1993 |
Externally published | Yes |
ASJC Scopus subject areas
- Microbiology