ATCase catalyzes the conversion of carbamoyl phosphate and aspartate into N-carbamoylaspartate, a precursor in pyrimidine biosynthesis. What roles do ATP and CTP play in this reaction? uncompetitive inhibitors heterotropic modulators homotropic modulators mixed inhibitors
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- Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.PLP can catalyze both \alpha, \beta elimination reactions and \beta, \gamma - elimination reactions. Propose a mechanism for the following PLP - catalyzed \beta, \gamma elimination
- Which of the following regulatory mechanisms will specifically inhibit pyrimidine synthesis (and not also purine synthesis)? (A) allosteric regulation of aspartate transcarbamoylase by CTP(B) allosteric regulation of aspartate transcarbamoylase by ATP(C) synergistic inhibition of PRPP synthetase by AMP/GMP/IMP(D) synergistic inhibition of PRPP amidotransferase by AMP/GMP/IMP (E) feedback inhibition of ribonucleotide reductase by dATPTrypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-alaPhosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because itmimics the two physiological substrates of the enzyme. However, in the presence of substrates, lowconcentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.
- You are subsequently instructed to improve the biochemical function of pyruvate kinase,which aids in the conversion of phosphoenolpyruvate to pyruvate. Suggest an approach thatcan be conducted to achieve this goal. Compare the approach that you have chosen withother existing procedures, such as construction of mutant enzymes.can somone please List the components of the enzyme complex involved in the transition step and Simply describe what does each component does? 1. 2. 3. ect..What is the evidence that aspartate transcarbamoylase (ATCase) effects catalysis primarily by proximity? In the figure, what is the role of Lys 84' in the active site- interaction that appear to make with the substrate?
- The following are the negative regulators of phosphofructokinase except Select one: a. AMP +b. H c. Citrate d. ATPFollowing this experiment, you would like to elucidate the mechanism of action of pyruvatekinase. Unfortunately, the crystal structure of pyruvate kinase is not available, whichrequires the enzyme to be modelled based on the available three-dimensional structures ofrelated enzymes. Suggest a bioinformatics approach that can be conducted to perform thisstudy.There is an enzyme that catalyzes the production of the pigment responsible for dark fur color in Siamese cats and Himalayan rabbits. This enzyme is thermolabile, meaning that it does not function at higher temperatures. Rabbits raised at 5°C are all black. If raised at 20°C, they are white with black paws, ears, and noses; they are all white when raised at 35°C. Draw an activity curve for this enzyme.