help me please

Multiple Choice 1 point E. coli aspartate transcarbamoylase synthesizes the pyrimidine ring of cytosine uracil, thymine The allosteric inhibitor CTP binds to a site different from the active site to inhibit enzyme function Why is CTP a good inhibitor? (Cytosine tri-phsophate) ON OFF CTP bound CTP molecule 5 nm active site ACTIVE ENZYME INACTIVE ENZYME It is the product of the reaction It's plentiful in the cell OOOO If there's a lot of CTP it suggests there are enough pyrimidines in the cell CTP-->CDP has a -delta G so can be coupled to the reaction to drive it forward. 10 Multiple Choice 1 point Phosphofructokinase attaches a phosphate to fructose 6 phosphate (third step in glycolysis). It binds ATP in two places - the catalytic site (or active site) and the allosteric binding site. Allosteric binding by ATP inhibits the enzyme. Which should have a higher Kd? O The active site O The allosteric site