Azotobacter Vinelandii Citrate Synthase

Magali Rault-Leonardon, Paul A. Srere, Mark A.L. Atkinson, Clive A. Slaughter, Carolyn R. Moomaw

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Abstract

We have purified the citrate synthase from Azotobacter vinelandii and have determined that the size of the subunit is 48 000 Da and the structure of the holoenzyme is a hexamer. This contrasts with earlier estimates that indicate a 58 000 Da subunit and a tetrameric structure. In addition, the enzyme is allosteric with a Hill coefficient of 1.5 and is inhibited by NADH. The Hill coefficient is changed to about 1 by high ionic strength and AMP. The enzyme is thus similar to the citrate synthases of many other Gram-negative, facultative, anaerobic organisms. In addition, the amino acid sequence of about 100 residues has been determined and found to be highly similar to the sequence of Pseudomonas aeruginosa citrate synthase.

Original languageEnglish
Pages (from-to)257-263
Number of pages7
JournalBiochemistry
Volume34
Issue number1
DOIs
Publication statusPublished - Jan 1 1995

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Rault-Leonardon, M., Srere, P. A., Atkinson, M. A. L., Slaughter, C. A., & Moomaw, C. R. (1995). Azotobacter Vinelandii Citrate Synthase. Biochemistry, 34(1), 257-263. https://doi.org/10.1021/bi00001a031