This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hobert, E H Articles by Datta, P Search for Related Content PubMed PubMed Citation Articles by Hobert, E H Articles by Datta, P

 Previous Article  |  Next Article 

J Bacteriol. 1983 August; 155(2): 586-592

Synthesis of biodegradative threonine dehydratase in Escherichia coli: role of amino acids, electron acceptors, and certain intermediary metabolites.

ABSTRACT

The specific activity of inducible biodegradative threonine dehydratase (EC 4.2.1.16) in Escherichia coli K-12 increased significantly when the standard tryptone-yeast extract medium or a synthetic mixture of 18 L-amino acids was supplemented with 10 mM KNO3 or 50 mM fumarate and with 4 mM cyclic AMP. In absolute terms, almost four times as much enzyme was produced in the amino acid medium as in the tryptone-yeast extract medium. Enzyme induction in the amino acid medium was sensitive to catabolite repression by glucose, gluconate, glycerol, and pyruvate. An analysis of amino acid requirements for enzyme induction showed that a combination of only four amino acids, threonine, serine, valine, and isoleucine, produced high levels of threonine dehydratase provided that both fumarate and cyclic AMP were present. Immunochemical data revealed that the enzyme synthesized in the presence of these four amino acids was indistinguishable from that produced in the tryptone-yeast extract or the medium with 18 amino acids. We interpret these results to mean that not the amino acids themselves but some metabolites derived anaerobically in reactions involving an electron acceptor may function as putative regulatory molecule(s) in the anaerobic induction of this enzyme.

This article has been cited by other articles:

• Ogawa, W., Kim, Y.-M., Mizushima, T., Tsuchiya, T. (1998). Cloning and Expression of the Gene for the Na+-Coupled Serine Transporter from Escherichia coli and Characteristics of the Transporter. J. Bacteriol. 180: 6749-6752 [Abstract] [Full Text]  
• Sawers, G., Heßlinger, C., Muller, N., Kaiser, M. (1998). The Glycyl Radical Enzyme TdcE Can Replace Pyruvate Formate-Lyase in Glucose Fermentation. J. Bacteriol. 180: 3509-3516 [Abstract] [Full Text]