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. 1995 Jan 10;34(1):257-63.
doi: 10.1021/bi00001a031.

Azotobacter vinelandii citrate synthase

M Rault-Leonardon  1 , M A Atkinson, C A Slaughter, C R Moomaw, P A Srere
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Azotobacter vinelandii citrate synthase

M Rault-Leonardon et al. Biochemistry. .

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.

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