Pyruvate dehydrogenase activity in Streptococcus mutans.
Streptococcus mutans NCTC 10449 and Escherichia coli K-12 strain 37 were grown under aerobic and anaerobic conditions. In cell extracts of both strains, pyruvate dehydrogenase activity dependent on thiamine pyrophosphate, coenzyme A, and NAD was shown. The enzyme was induced by pyruvate in the growth medium, and there was higher activity in aerobically grown cells than in anaerobically grown cells. Acetyl phosphate was a potent inhibitor of the activity. This inhibition was partly overcome by inorganic phosphate.
D005292:Ferricyanides / Q000378:metabolism; D010710:Phosphates / Q000494:pharmacology; D011768:Pyruvate Dehydrogenase Complex / Q000032:analysis*; D013295:Streptococcus mutans / Q000201:enzymology*
D005292:Ferricyanides; D010710:Phosphates; D011768:Pyruvate Dehydrogenase Complex; C007931:hexacyanoferrate III