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.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
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