This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Roon, R. J. Articles by Barker, H. A. Search for Related Content PubMed PubMed Citation Articles by Roon, R. J. Articles by Barker, H. A.

 Previous Article  |  Next Article 

J Bacteriol. 1972 January; 109(1): 44-50
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Fermentation of Agmatine in Streptococcus faecalis: Occurrence of Putrescine Transcarbamoylase

Department of Biochemistry, University of California, Berkeley, California 94720

ABSTRACT

Putrescine transcarbamoylase, EC 2.1.3.x (carbamoylphosphate:putrescine transcarbamoylase), has been purified from Streptococcus faecalis 10C1 grown on agmatine as primary energy source. The formation of N-carbamoylputrescine from putrescine and carbamoylphosphate serves as a convenient and sensitive assay for this enzymatic activity. The enzyme catalyzes both the phosphorolysis arsenolysis of N-carbamoylputrescine. Arginine does not induce the synthesis of putrescine transcarbamoylase in S. faecalis. Furthermore, the putrescine transcarbamoylase activity is easily separated from ornithine transcarbamoylase activity by gel filtration on Sephadex G-100 indicating that the two activities are associated with different proteins. The significance of this new enzyme in the fermentation of agmatine and its relation to the other known transcarbamoylases are discussed.

This article has been cited by other articles:

• Llacer, J. L., Polo, L. M., Tavarez, S., Alarcon, B., Hilario, R., Rubio, V. (2007). The Gene Cluster for Agmatine Catabolism of Enterococcus faecalis: Study of Recombinant Putrescine Transcarbamylase and Agmatine Deiminase and a Snapshot of Agmatine Deiminase Catalyzing Its Reaction. J. Bacteriol. 189: 1254-1265 [Abstract] [Full Text]  
• Griswold, A. R., Jameson-Lee, M., Burne, R. A. (2006). Regulation and Physiologic Significance of the Agmatine Deiminase System of Streptococcus mutans UA159. J. Bacteriol. 188: 834-841 [Abstract] [Full Text]  
• Griswold, A. R., Chen, Y.-Y. M., Burne, R. A. (2004). Analysis of an Agmatine Deiminase Gene Cluster in Streptococcus mutans UA159. J. Bacteriol. 186: 1902-1904 [Abstract] [Full Text]