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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
