Partial Purification and Properties of Citrate Synthases from the Thermoacidophilic Archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius

  • Grossebüter W
  • Görisch H
  • 4


    Mendeley users who have this article in their library.
  • 15


    Citations of this article.


Archaebacterial citrate synthases were partially purified from the thermoacidophiles Thermoplasma acidophilum and Sulfolobus acidocaldarius. The enzyme from T. acidophilum was purified 38-fold. It showed a Kmvalue of 6.3 × 10-6M for acetyl-CoA and of 4.1 × 10-6M for oxaloacetate. Citrate synthase from S. acidocaldarius was purified 70-fold; its Kmvalues were found to be 10-5M for acetyl-CoA and 2.6 × 10-5M for oxaloacetate. ATP, NADH and NADPH inhibited both enzymes competitively with respect to acetyl-CoA. The sensitivity of the enzymes from both archaebacteria towards NADH was low while NADPH showed stronger inhibitory effects. Both enzymes possess a molecular weight of about 70 000 as estimated by gel filtration methods. The citrate synthases from both thermoacidophilic archaebacteria resembled more closely the enzymes found in Gram-positive eubacteria and in eukaryotes rather than the enzymes from Gram-negative eubacteria. © 1985, Gustav Fischer Verlag, Stuttgart/New York. All rights reserved.

Author-supplied keywords

  • Archaebacteria
  • Citrate synthase
  • Purification
  • Regulation
  • Sulfolobus acidocaldarius
  • Thermoplasma acidophilum

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Wilhelm Grossebüter

  • Helmut Görisch

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free