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. 1979 Jul;25(1):157–163. doi: 10.1128/iai.25.1.157-163.1979

Pyruvate oxidation by Treponema pallidum.

J T Barbieri, C D Cox
PMCID: PMC414432  PMID: 383612

Abstract

Cell-free extracts of Treponema pallidum catalyzed the decarboxylation of pyruvate. This activity was suppressed at low O2 tensions and appeared to be coenzyme A independent. Pyruvate decarboxylation was inorganic phosphate dependent, and evidence suggested that acetyl phosphate was a product. Oxygen was consumed, and data indicated that H2O2 was produced. These results indicated that the overall oxidation of pyruvate was: pyruvate + O2 + inorganic phosphate leads to CO2 + acetyl phosphate + H2O2. Phosphotransacetylase and acetate kinase activities were also observed in the cell-free extracts and could catalyze formation of acetyl coenzyme A and adenosine 5'-triphosphate, respectively, from acetyl phosphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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