WebDuring the allosteric regulation of the bacterial enzyme aspartate transcarbamoylase (ATCase), two different allosteric regulators affect the activity of the enzyme on its substrate aspartate. CTP (cytidine triphosphate) _____ ATCase activity, while ATP (adenosine triphosphate) _____ ATCase activity. WebJan 27, 2016 · Aspartate Transcarbamoylase (ATCase) is an allosterically regulated enzyme with unique quaternary structure involving separable catalytic and regulatory subunits. …
Aspartate Transcarbamoylase (ATCase) - Kenyon College
WebThe inhibitor CTP binds preferentially to the ___ state of ATCase t The metabolic significance of the activation of ATCase by __________ is that it tends to coordinate the rates of synthesis of purines and pyrimidines. ATP The effects of uncompetitive inhibition on Vmax are not reversed by increasing substrate concentration. True WebRegulatory subunit binds to ATP and CTP but does not have any detectable ATCase activity. Reconstituion of regulatory and catalytic subunits (after the removal of mercurial) generates the fully fiunctional ATCase. Catalytic and regulatory sites are located on different subunits of ATCase. cpwd up lucknow tender
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WebMar 6, 2024 · ATCase [aspartate transcarbamoylase] catalyzes the first step in pyrimidine biosynthesis. In bacteria pyrimidine nucleotide biosynthesis is regulated by a feedback … WebNov 16, 2016 · Cytidine triphosphate (CTP), which is an end product of the pyrimidine biosynthetic pathway, has a negative allosteric effect on ATCase activity, while adenosine triphosphate, ATP, has a positive … WebScheduling and Locations CTP - afponline.org distressed floating driftwood shelves