Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification

Q: p. The forward reaction would be written as: Please select the correct letters from graph (a-e) to…

A: Enzymes are biological catalyst. It catalysed all biological reactions that maintains homeostasis.…

Q: Which of the substrates is likely to have a higher Vmax. What is your reasoning? e. Can you propose…

A: d. Km is the substrate concentration at which Vmax is half. Substrate with higher Km will have high…

Q: B) Uncompetitive inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme…

A: An enzyme inhibitor is a molecule that will bind to an enzyme to decrease or slow down its activity.…

Q: Many pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false…

A: Enzyme inhibition occurs when certain substances, called inhibitors bind to and inactivate enzymes.…

Q: Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified…

A: Enzyme inhibitors are the molecules are the chemical compounds that bind to the enzyme to influence…

Q: A.   Estimate from the graph what the Vmax is for the enzyme without inhibitor present (black…

A: According to the Michaelis–Menten equation, V is the velocity or rate of an enzyme-catalyzed…

Q: Metabolic flux is regulated by both availability of substrates and level of enzyme activity. Match…

A: Enzymes are proteins which increase the rate of biochemical reactions. They carry out the quick…

Q: I. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we…

A: A protein's tertiary structures are the result of canonical forces that stabilize protein structure.…

Q: A allosteric regulator the rate of an enzyme-catalyzed reaction by inducing the active site of the…

A: Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules…

Q: Which of the following statements is true? a. Plotting the rate of facilitated transport against…

A: Facilitated transport, also known as facilitated diffusion, is a mechanism of passive transport that…

Q: Enzyme X follows Michaelis-Menten kinetics. You add an inhibitor to your enzyme and you notice that…

A: The Michaelis-Menten equation is used to describe the kinetics of enzyme catalyzed reactions. It…

Q: C) Mixed inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme do…

A: Inhibitors are the substances which inhibit the enzymes from performing its catalytic role in the…

Q: T/F Both competitive and noncompetitive inhibitors bind reversibly to an enzyme (E), thereby…

A: Both competitive and noncompetitive inhibitors are reversible inhibitors which are the enzymes that…

Q: C. What types of inhibitors of this enzyme is shown below? (1). D. What effect (increase, decrease,…

A: Enzymes are a class of protein except for ribozymes (class of ribozymes) that elevates the chemical…

Q: Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the…

A: Enzymes are proteins which act as biocatalysts. Substrates bind with an enzyme at the active site.…

Q: significance of transition state stabilisation and how this impacts the free energy of activation in…

A: Transition state stabilization is crucial in enzyme-catalyzed reactions as it lowers the energy…

Q: Which statement is/are TRUE about inhibitors?   A. Mode of action of penicillin on bacteria is an…

A: Inhibitors are the molecules that show impact on the enzyme activity. They interact with Enzymes in…

Q: Explain and discuss an advantage and a disadvantage of regulating enzyme activity via allosteric…

A: Enzymes can be regulated by other molecules that either increase or reduce their activity. Molecules…

Q: For B in the answer it is mentioned, "If the allosteric regulators increased the affinity of the…

A: Phosphofructokinase 1 is an important rate limiting enzyme of glycolysis. It catalyses the third…

Q: II. While there are many different types of inhibitors, most have a very similar structure so they…

A: Enzymes are high molecular weight protein that catalyse biochemical reactions. They contain a active…

Q: A) Competitive inhibition: Where do these inhibitors bind? To what mechanistic form of the enzyme do…

A: The competitive inhibitor is a type of inhibition process in which an enzyme is analogous to the…

Q: Match the descriptions and compounds with the terms competitive, uncompetitive, and noncompetitive…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: A.What is the Result of the sodium potassium ATPase activity in the cell? B.What mechanism does the…

A: The plasma membrane contains the sodium-potassium pump.

Q: Consider the enzyme, ATCase. All are true except: It's K effectors are ATP and CTP It is a K…

A: ATCase (Aspartate carbamoyltransferase) is an enzyme which catalyzes the first step of the synthesis…

Q: IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide…

A: Insulin is a hormone responsible for the regulation of sugar levels in the blood. Insulin hormone is…

Q: The induced-fit theory aims to explain how the interactions between an enzyme and a sub- strate…

A: Enzymes are highly specific biocatalysts. Enzymes are specialized proteins or sometimes RNA which…

Q: A.  Which enzyme model involves the enzyme staying the same shape when the substrate binds to it?…

A: Enzymes are biomolecules that act as catalysts. These are substances that speed up the chemical…

Q: What are the effects of different light colors in photosynthesis? O Different light colors will…

A: Photosynthesis is the phenomenon by which green plants and other organisms prepare food. They…

Q: Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to…

A: Henderson-Hasselbalch equation relates pH, pKa and the ratio of  concentrations of protonated to…

Q: Feedback inhibition of enzyme activity is, as we discussed in class, generally thought to represent…

A: Introduction: The correct choice is option D. allosteric

Q: Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and…

A: Regulatory enzymes exhibit increased or decreased catalytic activity in response to specific…

Q: equations and values: E can bind to two different substrates, S and I. The binding reactions are…

A: The protein that acts as a biological catalyst by accelerating chemical reactions is known as…

Q: Describe the categories of enzyme control: (image provided) Allosteric control with example…

A: There are 4 general methods that mechanism cells use to control enzymes. These are allosteric,…