Abstract
The mitochondrial-associated CTP: phosphatidic acid cytidylyltransferase (CDP-diacylglycerol synthase, EC 2.7.7.41) was studied from germinating soybeans. The enzyme exhibited a broad pH optimum between pH 6.5 and pH 8.0. Activity was dependent on the addition of magnesium ions (20 mM) and the nonionic detergent Triton X-100 (5 mM). The apparent Km values for CTP and phosphatidic acid were 0.58 mM and 0.12 mM, respectively. A Vmax of 0.12 U/mg was found for the mitochondrial-associated enzyme. Phospholipids generally stimulated activity while ADP and CDP strongly inhibited activity. Thiore-active agents inhibited activity indicating that a sulphydryl group is essential for activity. The enzyme was thermally inactivated at temperatures above 35°C.
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.
