Regulation of dihydrodipicolinate synthase and aspartate kinase in Bacillus subtilis.

Abstract

The regulation of dihydrodipicolinate synthase (EC 4.2.1.52) and aspartate kinase (EC 2.7.2.4) was studied in Bacillus subtilis 168. Starvation for lysine gave depression of one aspartate kinase isoenzyme but not of dihydrodipicolinate synthase. Strains resistant to growth inhibition by the lysine analogue thiosine exhibited constitutively derepressed synthesis of one aspartate kinase isoenzyme but had normal levels of dihydrodipicolinate synthase. The data provide strong evidence that lysine is not the signal for derepression of dihydrodipicolinate synthase. Nevertheless, dihydrodipicolinate synthase specific activity increased during sporulation, and it is suggested that this increase may result, in part, from resistance to proteolysis of that enzyme.

• Authors: B Vold, J Szulmajster, A Carbone
• Journal: Journal of bacteriology (J Bacteriol) Vol. 121 Issue 3 Pg. 970-4 (Mar 1975) ISSN: 0021-9193 [Print] United States
• PMID: 163819 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Picolinic Acids
• Aspartic Acid
• Phosphotransferases
• Hydro-Lyases
• Lysine

Topics

• Aspartic Acid
• Bacillus subtilis (drug effects, enzymology, growth & development)
• Drug Resistance, Microbial
• Enzyme Repression
• Hydro-Lyases (metabolism)
• Lysine (analogs & derivatives, metabolism, pharmacology)
• Mutation
• Phosphotransferases (metabolism)
• Picolinic Acids
• Spores, Bacterial (enzymology, growth & development)