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  • Title: Purification and characterization of phosphoenolpyruvate carboxykinase,a catabolic CO2-fixing enzyme, from Anaerobiospirillum succiniciproducens.
    Author: Podkovyrov SM, Zeikus JG.
    Journal: J Gen Microbiol; 1993 Feb; 139(2):223-8. PubMed ID: 8436945.
    Abstract:
    Phosphoenolpyruvate (PEP) carboxykinase (EC 4.1.1.49) from the obligate anaerobe Anaerobiospirillum succiniciproducens was purified 18-fold. The enzyme was monomeric, with an Mr of 57,000 +/- 2,000. The enzyme was oxygen stable, had a pH optimum of 6.7-7.1, 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 Km of 0.54 mM, 17 mM and 0.42 mM, respectively. The enzyme required Mn(2+) or Co(2+) in addition to Mg(2+) to exhibit maximum activity. p-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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