Abstract
Abstract The multiple inhibition technique is used to show that substrate inhibition by α-ketoglutarate results from combination with central complexes and inhibition of catalysis or product release, and not from dead-end combination with E-TPN. Oxalylglycine (an analogue of α-ketoglutarate) is a good dead-end inhibitor competitive versus both α-ketoglutarate and isocitrate and noncompetitive versus TPN. These patterns, and the results of multiple inhibition studies with oxalylglycine and TPNH, show conclusively that the mechanism of TPN-isocitrate dehydrogenase must be random.
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 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.
