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- Title
Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.
- Authors
Deutscher, Josef; Saier, Milton H, Jr
- Abstract
The first clearly established example of Ser/Thr/Tyr phosphorylation of a bacterial protein was isocitrate dehydrogenase. In 1979, 25 years after the discovery of protein phosphorylation in eukaryotes, this enzyme was reported to become phosphorylated on a serine residue. In subsequent years, numerous other bacterial proteins phosphorylated on Ser, Thr or Tyr were discovered and the corresponding protein kinases and P-protein phosphatases were identified. These protein modifications regulate all kinds of physiological processes. Ser/Thr/Tyr phosphorylation in bacteria therefore seems to play a similar important role as in eukaryotes. Surprisingly, many bacterial protein kinases do not exhibit any similarity to eukaryotic protein kinases, but rather resemble nucleotide-binding proteins or kinases phosphorylating diverse low-molecular-weight substrates.
- Publication
Journal of molecular microbiology and biotechnology, 2005, Vol 9, Issue 3-4, p125
- ISSN
1464-1801
- Publication type
Journal Article
- DOI
10.1159/000089641