Purification and characterization of phosphoenolpyruvate carboxykinase, a catabolic CO2-fixing enzyme, from Anaerobiospirillum succiniciproducens
Podkovyrov, Sergey M. and Zeikus, J. Gregory,, 139, 223-228 (1993),
doi = https://doi.org/10.1099/00221287-139-2-223,
publicationName = Microbiology Society,
issn = 1350-0872,
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 M r 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 K m of 0·54 mm, 17 mm and 0·42 mm, respectively. The enzyme required Mn2+ or Co2+ in addition to Mg2+ 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.,
language=,
type=