Archives of Microbiology

, Volume 152, Issue 6, pp 584–588

Isolation and characterization of oxaloacetate decarboxylase of Salmonella typhimurium, a sodium ion pump

  • Klaus Wifling
  • Peter Dimroth
Original Papers

DOI: 10.1007/BF00425491

Cite this article as:
Wifling, K. & Dimroth, P. Arch. Microbiol. (1989) 152: 584. doi:10.1007/BF00425491


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 α, β, γ, with apparent molecular weights of 63800, 34500 and 10600. The α-chain contains a covalently attached biotin group and binds to antibodies raised against the α-subunit of oxaloacetate decarboxylase from Klebsiella pneumoniae. The Na+ transport function was reconstituted by incorporation of the puriried enzyme into proteoliposomes.

Key words

Citrate fermentation Oxaloacetate decarboxylase Salmonella typhimurium Sodium transport 

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • Klaus Wifling
    • 1
  • Peter Dimroth
    • 1
  1. 1.Institut für Physiologische Chemie der Technischen Universität MünchenMünchen 40Germany

Personalised recommendations