Biotechnology Bulletin ›› 2013, Vol. 0 ›› Issue (7): 172-178.

• Study Report • Previous Articles     Next Articles

Phosphoenolpyruvate Carboxylase from Corynebacterium glutamicum Inhibited by Diverse Biochemicals

Wu Xinyang1,3 Pei Guangsheng 1,3 Zheng Xiaomei2,3 Cao Guoqiang2,3 Liu Jiao2,3 Zheng Ping2,3 Wang Min1 Sun Jibin2,3   

  1. (1. School of Biological Engineering,Tianjin University of Science and Technology,Tianjin 300457;2. Key Laboratory of Systems Microbial Biotechnology,Chinese Academy of Sciences,Tianjin 300308;3. Tianjin Institute of Industrial Biotechnology,Chinese Academy of Sciences,Tianjin 300308)
  • Received:2013-01-04 Revised:2013-07-19 Online:2013-07-19 Published:2013-09-02

Abstract: Phosphoenolpyruvate carboxylase(PPC), an enzyme involved in replenishment of the four-carbon dicarboxylic acid intermediate pool of the TCA cycle, plays an important role in both biological and biotechnological synthesis pathways. To discover the effect of diverse inhibitors on the activity of PPC, the full-length sequence of the ppc gene from Corynebacterium glutamicum ATCC13032 was cloned and expressed as soluble form in Escherichia coli. The recombinant PPC was purified with Ni-Column. The purified enzyme showed high phosphoenolpyruvate carboxylase activity, and was inhibited by diverse inhibitors such as citrate, isocitrate, fumarate, glutamate, aspartate, malate etc. Aspartate and malate were the strongest inhibitors. For the first time, the inhibition of PPC activity by N-acetyl glutamine was clearly demonstrated in a glutamate-producing strain of C. glutamicum.

Key words: Phosphoenolpyruvate carboxylase, Corynebacterium glutamicum, Inhibitor, N-acetyl glutamine.