Pyruvate oxidation by Treponema pallidum.
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.
D000084:Acetate Kinase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D010101:Oxygen Consumption; D010709:Phosphate Acetyltransferase / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D011767:Pyruvate Decarboxylase / Q000378:metabolism; D011773:Pyruvates / Q000378:metabolism*; D014210:Treponema pallidum / Q000378:metabolism*
D010710:Phosphates; D011773:Pyruvates; D006861:Hydrogen Peroxide; D010709:Phosphate Acetyltransferase; D000084:Acetate Kinase; D011767:Pyruvate Decarboxylase