The second aconitase (AcnB) of Escherichia coli
Article Abstract:
The partial purification of the second aconitase (AcnB) of Escherichia coli from the acnA::kan super R mutant, the identification of the acnB gene and the purification of AcnB from amplified sources to near homogeneity are described. AcnB, which is related to AcnA, shows a domain rearrangement relative to AcnA and other aconitases. The sequence identity between AcnA and AcnB is a mere 17%. The domain organization of AcnA and related proteins, which is 1-2-3-linker-4, is reconfigured in AcnB to 4-1-2-3.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Construction and properties of aconitase mutants of Escherichia coli
Article Abstract:
A comparison of the properties of acnB and acnAB single and double mutants and acnA mutant was conducted to define the role of AcnA and AcnB in Escherichia coli. Results reveal that aerobic and anaerobic growth in glucose minimal medium were impaired but not abolished by acnB mutation, Furthermore, results show that there is a notable retention of a low residual aconitase activity in the acnAB double mutant.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli
Article Abstract:
A study was conducted on the transcriptional organization of the aconitase genes of Escherichia coli, acnA and acnB, using Northern blot hybridization. The findings indicate that AcnB is an important citric acid cycle enzyme while AcnA is an aerobic stationary-phase enzyme induced by redox-stress and iron. Further studies are recommended on the characterization of the putative third aconitase, AcnC.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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