Affiliation:
1. 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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference18 articles.
1. Oxamic transcarbamylase of Streptococcus auantoicus;Bojanowski R.;J. Bacteriol.,1964
2. A simple efficient liquid scintillator for counting aqueous solution in a liquid scintillation counter;Bray G. E.;Anal. Biochem.,1960
3. Study of carbamyl phosphate-ornithine transcarbamylase;Burnett G. H.;J. Biol. Chem.,1957
4. Cohen P. P. and M. Marshall. 1962. Carbamyl group transfer p. 327-338. In P. D. Boyer H. Lardy and K. Myrback (ed.) The enzymes vol. 6. Academic Press Inc. New York.
5. Utilization of arginine as an energy source for the growth of Streptococcus faecalis;Deibel R. H.;J. Bacteriol.,1964
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