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Journal of Bacteriology, August 1998, p. 4278-4286, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Arginine Catabolism and the Arginine Succinyltransferase Pathway in Escherichia coli

Barbara L. Schneider,dagger Alexandros K. Kiupakis, and Lawrence J. Reitzer*

Department of Molecular and Cell Biology, The University of Texas at Dallas, Richardson, Texas 75083-0688

Received 11 September 1997/Accepted 3 June 1998

Arginine catabolism produces ammonia without transferring nitrogen to another compound, yet the only known pathway of arginine catabolism in Escherichia coli (through arginine decarboxylase) does not produce ammonia. Our aims were to find the ammonia-producing pathway of arginine catabolism in E. coli and to examine its function. We showed that the only previously described pathway of arginine catabolism, which does not produce ammonia, accounted for only 3% of the arginine consumed. A search for another arginine catabolic pathway led to discovery of the ammonia-producing arginine succinyltransferase (AST) pathway in E. coli. Nitrogen limitation induced this pathway in both E. coli and Klebsiella aerogenes, but the mechanisms of activation clearly differed in these two organisms. We identified the E. coli gene for succinylornithine aminotransferase, the third enzyme of the AST pathway, which appears to be the first of an astCADBE operon. Its disruption prevented arginine catabolism, impaired ornithine utilization, and affected the synthesis of all the enzymes of the AST pathway. Disruption of astB eliminated succinylarginine dihydrolase activity and prevented arginine utilization but did not impair ornithine catabolism. Overproduction of AST enzymes resulted in faster growth with arginine and aspartate. We conclude that the AST pathway is necessary for aerobic arginine catabolism in E. coli and that at least one enzyme of this pathway contributes to ornithine catabolism.

* Corresponding author. Mailing address: Department of Molecular and Cell Biology, Mail Station FO 3.1, The University of Texas at Dallas, P.O. Box 830688, Richardson, TX 75083-0688. Phone: (972) 883-2523. Fax: (972) 883-2409. E-mail: reitzer{at}utdallas.edu.

dagger Present address: Department of Biology, University of California at San Diego, La Jolla, CA 92093-0116.

Journal of Bacteriology, August 1998, p. 4278-4286, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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