Summary: Phosphoenolpyruvate (PEP) carboxykinase (EC from the obligate anaerobe was purified 18-fold. The enzyme was monomeric, with an of 57000 ± 2000. The enzyme was oxygen stable, had a pH optimum of 6.5-7.1, and was stable from pH 5.0 to 9.0. The enzyme displayed Michaelis-Menten kinetics for the substrate PEP and the cosubstrates bicarbonate and ADP with a of 0.54 mM, 17 mM and 0.42 mM, respectively. The enzyme required Mn or Co in addition to Mg to exhibit maximum activity. -Chloromercuribenzoate inhibited activity and phosphoenolpyruvate protected the enzyme against inactivation, suggesting that an essential cysteine may be in the active site.


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