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PMID: 6143742 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

2-Ketoglutarate and the regulation of aconitase and histidase formation in Bacillus subtilis.

Journal of bacteriology ·Vol. 158 ·No. 1 ·1984-04-00 ·Pages 379-82

Fisher SH, Magasanik B

Abstract

In contrast to wild-type cells, the Bacillus subtilis mutant SF109 that lacks the active 2-ketoglutarate dehydrogenase enzymatic complex is unable to increase the specific activity of two enzymes subject to glucose catabolite repression, aconitase and histidase, during limitation of growth by glucose. Examination of the intracellular metabolite pools in the mutant and wild-type cells grown in excess and limiting glucose medium showed that the complete derepression of aconitase and histidase could be correlated with the decrease in the intracellular concentration of 2-ketoglutarate. The complete repression of aconitase that occurred in wild-type and mutant cells could be correlated with a high intracellular concentration of 2-ketoglutarate.

MeSH Terms
Aconitate Hydratase/biosynthesis Ammonia-Lyases/biosynthesis Aspartic Acid/metabolism Bacillus subtilis/enzymology,genetics,growth & development Enzyme Repression Glucose/metabolism Glutamates/metabolism Glutamic Acid Histidine Ammonia-Lyase/biosynthesis Ketoglutaric Acids/metabolism Mutation
Chemicals
Glutamates Ketoglutaric Acids Aspartic Acid Glutamic Acid Aconitate Hydratase Ammonia-Lyases Histidine Ammonia-Lyase Glucose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fisher S H
Magasanik B
References (11)
11 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1984-04-00
Pages
379-82
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC215431
Subset
IM
Grants
NIAID NIH HHS · 5F32AI05711 · United States
NIADDK NIH HHS · AM-13894 · United States
NIGMS NIH HHS · GM-07446 · United States
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