1887

Abstract

Phosphoenolpyruvate (PEP) carboxykinase (EC 4.1.1.49) 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 m, 17 m and 0·42 m, 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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1993-02-01
2024-04-20
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