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Current Microbiology

, Volume 22, Issue 1, pp 73–76 | Cite as

Regulation of isocitrate lyase inRhodobacter capsulatus E1F1

  • Rafael Blasco
  • Jacobo Cárdenas
  • Francisco Castillo
Article

Abstract

InRhodobacter capsulatus E1F1, isocitrate lyase (ICL) (EC 4.5.3.1) is a regulatory enzyme whose levels are increased in the presence of acetate as the sole carbon source. Acetate activated isocitrate lyase in a process dependent on energy supply and de novo protein synthesis. In contrast to isocitrate lyase, isocitrate dehydrogenase (ICDH) activity was independent of the carbon source used for growth and significantly increased in darkened cells. Pyruvate or yeast extract prevented in vivo activation of isocitrate lyase in cells growing on acetate. The enzyme was reversibly inactivated to a great extent in vitro by pyruvate and other oxoacids presumably involved in acetate metabolism. These results suggest that, inR. capsulatus E1F1, isocitrate lyase is regulated by both enzyme synthesis and oxoacid inactivation.

Keywords

Enzyme Acetate Carbon Source Protein Synthesis Pyruvate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 1991

Authors and Affiliations

  • Rafael Blasco
    • 1
  • Jacobo Cárdenas
    • 1
  • Francisco Castillo
    • 1
  1. 1.Departmento de Bioquímica y Biología Molecular y Fisiología, Facultad de Ciencias, Avda. San Alberto Magno s/nUniversidad de CórdobaCórdobaSpain

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