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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- UDP-glucose pyrophosphorylase catalyzes the removal of a pyrophosphate group from UTP as it synthesizes UDP-glucose. Why is this necessary, from a biochemical perspective? Both of the phosphate groups from UTP are needed to form UDP-glucose. There is no particular reason: wasteful reactions just happen sometimes. The pyrophosphate (after hydrolysis) is required to free up more phosphate for the synthesis of ATP by oxidative phosphorylation. The subsequent hydrolysis of pyrophosphate is a highly exergonic reaction, which pulls the equilibrium over towards UDP-glucose. Pyrophosphate is an allosteric activator of glycogen synthase, so this helps glycogen synthesis to proceed at a faster rate.The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATETrypsin 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-ala
- 6-Mercaptopurine , after its conversion to the corresponding nucleotide through salvage reactions, is a potent competitive inhibitor of IMP in the pathways for AMP and GMP biosynthesis. It is therefore a clinically useful anticancer agent. The chemotherapeutic effectiveness of 6 mercaptopurine is enhanced when it is administered with allopurinol. Explain the mechanism of this enhancement.The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.Fructose 2,6-bisphosphate is a potent stimulator of phosphofructokinase. Explain how fructose 2,6-bisphosphate might function in the concerted model for allosteric enzymes.
- Using the principles described in the text regarding pyridoxal phosphate mechanisms, propose a mechanism for the reaction catalyzed by serine hydroxymethyltransferase.Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.One of the regulators of the TCA cycle is succinyl CoA. Discuss the rationale for this molecule to be used to regulate the TCA cycle [include chemical structures and chemical equations where appropriate]. What is an allosteric inhibitor? How does it operate? For what TCA enzymes does succinyl CoA act as an inhibitor? What is the metabolic role of succinyl CoA? So then why is this molecule a reasonable choice as an inhibitor of the TCA?
- The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by a deacylation reaction. What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenyl ester by chymotrypsin? The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate. The rates of the acylation and deacylation reactions are equal. The rate of the acylation reaction is slower than the rate of the deacylation reaction. The rate of the acylation reaction is faster than the rate of the deacylation reaction.Why does it make metabolic sense for UTP to inhibit carbamoyl phosphate synthetase II, whereas ATP activates the enzyme?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?