Abstract
Isocitrate lyase was partially purified from germinating spores of the fern Anemia phyllitidis. The enzyme requires Mg 2+ and thiol compounds for maximal activity and has a pH optimum between 6.5 and 7.5. The K m of the enzyme for threo-Δ s-isocitrate is 0.5 mM. Succinate inhibits the enzyme non-competitively ( K i . 1.8 mM). The increase of isocitrate lyase activity is closely correlated with the induction of the germination process. The fall of enzyme activity during germination is associated with the decline in triglyceride reserves.
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.
