title: Isolation and characterization of oxaloacetate decarboxylase of Salmonella typhimurium, a sodium ion pump.
abstract: Anaerobic growth of Salmonella typhimurium on citrate is Na+-dependent and requires induction of the necessary enzymes during a 20-40 h lag phase. The citrate fermentation pathway involves citrate lyase and oxaloacetate decarboxylase. The decarboxylase is a membrane-bound, Na+-activated, biotin-containing enzyme that functions as a Na+ pump. Oxaloacetate decarboxylase was isolated by affinity chromatography of a Triton X-100 extract of the bacterial membranes on avidin-Sepharose. The enzyme consists of three subunits alpha, beta, gamma, with apparent molecular weights of 63,800, 34,500 and 10,600. The alpha-chain contains a covalently attached biotin group and binds to antibodies raised against the alpha-subunit of oxaloacetate decarboxylase from Klebsiella pneumoniae. The Na+ transport function was reconstituted by incorporation of the purified enzyme into proteoliposomes.
authors.affiliation: Institut für Physiologische Chemie der Technischen Universität München, Federal Republic of Germany.
authors.forename: K
authors.initials: K
authors.lastname: Wifling
authors.forename: P
authors.initials: P
authors.lastname: Dimroth
mesh_terms: D002262:Carboxy-Lyases / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D008970:Molecular Weight; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000378:metabolism; D015222:Sodium Channels / Q000378:metabolism*
chemical_list: D015222:Sodium Channels; D002262:Carboxy-Lyases; C021916:oxaloacetate decarboxylase