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Staphylococcus aureus CidC Is a Pyruvate:Menaquinone Oxidoreductase
Xinyan Zhang1, Kenneth W Bayles1, Sorin Luca1
1Department of Pharmaceutical Sciences and ‡Department of Pathology & Microbiology, University of Nebraska Medical Center , Omaha, Nebraska 68198-5900, United States.
The Staphylococcus aureus CidC enzyme, crucial for bacterial programmed cell death (PCD), catalyzes pyruvate oxidation. Its activity increases at acidic pH and is linked to the cell membrane, aiding PCD induction.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- Staphylococcus aureus CidC enzyme plays a role in stationary phase cell death and biofilm development.
- Understanding metabolic processes in bacterial programmed cell death (PCD) is crucial.
Purpose of the Study:
- To gain insight into the catalytic properties of the Staphylococcus aureus CidC enzyme.
- To elucidate the biochemical and biophysical characteristics of CidC.
Main Methods:
- In vitro biochemical and biophysical analysis of CidC.
- Enzyme activity assays at varying pH and in the presence of different compounds.
- Proteolytic cleavage assays.
Main Results:
- CidC catalyzes the oxidative decarboxylation of pyruvate to acetate and CO2.
- CidC reduces menadione, suggesting a role in the S. aureus respiratory chain.
- CidC activity is enhanced at acidic pH, with aggregation and membrane binding, and optimal activity at pH 5.5-5.8.
Conclusions:
- CidC functions as a pyruvate:menaquinone oxidoreductase.
- CidC activity is induced at the cell membrane during cytoplasmic acidification, contributing to bacterial PCD.
- CidC's properties differ from its E. coli homolog, PoxB.
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