Abstract
The threonine deaminase formed under anaerobic conditions by Salmonella typhimurium is induced by l-serine and l-threonine, is catabolite repressible, requires cyclic adenosine 3′,5′-monophosphate for its synthesis and adenylic acid for optimal activity, and is immunologically different from biosynthetic threonine deaminase.
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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
- FREUNDLICH M., BURNS R. O., UMBARGER H. E. Control of isoleucine, valine, and leucine biosynthesis. I. Multivalent repression. Proc Natl Acad Sci U S A. 1962 Oct 15;48:1804–1808. doi: 10.1073/pnas.48.10.1804. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MARGOLIN P. Genetic fine structure of the leucine operon in Salmonella. Genetics. 1963 Mar;48:441–457. doi: 10.1093/genetics/48.3.441. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Phillips A. T., Wood W. A. The mechanism of action of 5'-adenylic acid-activated threonine dehydrase. J Biol Chem. 1965 Dec;240(12):4703–4709. [PubMed] [Google Scholar]
- Sanderson K. E. Linkage map of Salmonella typhimurium, edition IV. Bacteriol Rev. 1972 Dec;36(4):558–586. doi: 10.1128/br.36.4.558-586.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shizuta Y., Hayaishi O. Regulation of biodegradative threonine deaminase synthesis in Escherichia coli by cyclic adenosine 3',5'-monophosphate. J Biol Chem. 1970 Oct 25;245(20):5416–5423. [PubMed] [Google Scholar]
- UMBARGER H. E., BROWN B. Threonine deamination in Escherichia coli. II. Evidence for two L-threonine deaminases. J Bacteriol. 1957 Jan;73(1):105–112. doi: 10.1128/jb.73.1.105-112.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]