Carnitine resembles choline in the induction of cholinesterase, acid phosphatase, and phospholipase C and in its action as an osmoprotectant in Pseudomonas aeruginosa

@article{Lucchesi2004CarnitineRC,
  title={Carnitine resembles choline in the induction of cholinesterase, acid phosphatase, and phospholipase C and in its action as an osmoprotectant in Pseudomonas aeruginosa},
  author={Gloria I Lucchesi and Teresita A. Lisa and C{\'e}sar H Casale and Carlos Eduardo Domenech},
  journal={Current Microbiology},
  year={2004},
  volume={30},
  pages={55-60}
}
The present study demonstrates that under conditions of iso or hyperosmolarity, P. aeruginosa utilized carnitine as the carbon, nitrogen or carbon and nitrogen sources. As occurred in the case of choline, the bacteria synthesized cholinesterase (ChE), acid phosphatase (Ac.Pase) and phospholipase C (PLC) under any of these conditions and in the presence of high or low Pi concentrations.Carnitine acted as an osmoprotectant when the cells were grown in the presence of preferred carbon and nitrogen… Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
In this review, recent advances in the aerobic and anaerobic metabolic pathways as well as the use of carnitine as an electron acceptor have addressed some long-standing questions in the field. Expand
Differential requirements for processing and transport of short-chain versus long-chain O-acylcarnitines in Pseudomonas aeruginosa.
TLDR
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A Pseudomonas aeruginosa PAO1 acetylcholinesterase is encoded by the PA4921 gene and belongs to the SGNH hydrolase family.
TLDR
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Identification and characterization of a carnitine transporter in Acinetobacter baumannii
TLDR
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