1887

Abstract

Summary: 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 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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/content/journal/micro/10.1099/00221287-139-2-223
1993-02-01
2019-11-15
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-139-2-223
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