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Citrate lyase from Streptococcus diacetilactis

Association with its acetylating enzyme

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Abstract

Citrate lyase (EC 4.1.3.6) was purified 38-fold from cell-free extracts of Streptococcus diacetilactis. The enzyme was homogeneous in analytical ultracentrifugation and polyacrylamide gel electrophoresis

The final enzyme preparation contained acetate: HS-citrate lyase ligase—an acetylating enzyme which converts inactive HS-citrate lyase into enzymatically active acetyl-S-citrate lyase. This enzyme activity was purified 25-fold over the crude extract and seemed to be associated with citrate lyase. Partially purified citrate lyase from Leuconostoc citrovorum contained also its acetylating enzyme.

Purified citrate lyases from Klebsiella aerogenes and Rhodopseudomonas gelatinosa were devoid of acetylating enzyme activity.

The HS-form of citrate lyase from S. diacetilactis was completely acetylated and hence activated by incubation with ATP and acetate for 25 min at 25° C. The enzyme did not acetylate the HS-lyases from R. gelatinosa and K. aerogenes.

In contrast to the citrate lyases from R. gelatinosa and K. aerogenes the enzymes from S. diacetilactis and L. citrovorum showed onlya very weak reaction inactivation. It is assumed that this is due to the association of the acetylating enzymes with these lyases.

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Authors and Affiliations

  1. Institut für Mikrobiologie der Universität Göttingen, München, in Göttingen

    Angela Kümmel, Gudrun Behrens & Gerhard Gottschalk

  2. Institut für Mikrobiologie der Gesellschaft für Strahlen- und Umweltforschung mbH, München, in Göttingen

    Angela Kümmel, Gudrun Behrens & Gerhard Gottschalk

Authors
  1. Angela Kümmel
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  2. Gudrun Behrens
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  3. Gerhard Gottschalk
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Kümmel, A., Behrens, G. & Gottschalk, G. Citrate lyase from Streptococcus diacetilactis . Arch. Microbiol. 102, 111–116 (1975). https://doi.org/10.1007/BF00428354

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  • DOI: https://doi.org/10.1007/BF00428354

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