Affiliation:
1. Department of Molecular and Cell Biology, The University of Texas at Dallas, Richardson, Texas 75083-0688
Abstract
ABSTRACT
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
126 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献