Abstract
1.1. P-enolpyruvate carboxylase was partially purified from Plasmodium berghei and some of its properties have been elucidated.2.2. Results suggest that P-enolpyruvate carboxylase from plasmodia is also an allosteric enzyme.3.3. Unlike the bacterial enzyme, the carboxylase from plasmodia was not affected by acetylCoA, aspartate, fructose disphosphate, or cyclic AMP-3′,5′. The apparent Km values are as follows: 1·05 × 10−3 M PEP, 1 × 10−3 M Mg2+, 2·6 × 10−4 M Co2+ and 1·0 × 10−4 M Mn2+.4.5. A rapid loss of enzymic activity occurred in the presence of urea.5.6. P-enolpyruvate carboxylase activity was inhibited by ferrous, ferric, cupric, and mercuric ions. The Ki values for ferrous and ferric ions were calculated to be 1·45 × 10−3 M and 1·41 × 10−3 M, respectively.6.7. The Hill plots for the relation between the Mg2+ concentration and the activity in the presence of ferrous and ferric ions suggest more than one interacting site for binding of these ions to the enzyme.
Sign-in/Register to access full text options 
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 callMore From: Comparative Biochemistry and Physiology -- Part B: Biochemistry and Molecular Biology
Disclaimer: 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.
