Acarbose (structure see below) is an exo-a-glucosidase inhibitor that is being used as an oral anti-diabetic drug. LOH HO HO OH HO NH HO LOH OH HO OH Acarbose HO HO OH OH (ii) Draw the enzymatic active site given above with the inhibitor Acarbose included (molecule can be abbreviated to only include essential parts) and use this presentation to explain the inhibitor properties of the drug. (20)

Acarbose (structure see below) is an exo-a-glucosidase inhibitor that is being used as an oral anti-diabetic drug. LOH HO HO OH HO NH HO LOH OH HO OH Acarbose HO HO OH OH (ii) Draw the enzymatic active site given above with the inhibitor Acarbose included (molecule can be abbreviated to only include essential parts) and use this presentation to explain the inhibitor properties of the drug. (20)

Organic Chemistry

8th Edition

ISBN:9781305580350

Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Chapter18: Functional Derivatives Of Carboxylic Acids

Section18.8: Interconversion Of Functional Derivatives

Problem BQ: Several compounds have been found to inhibit -lactamase, and drugs based on these compounds can be...

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Several compounds have been found to inhibit -lactamase, and drugs based on these compounds can be taken in combination with penicillins and cephalosporins to restore their effectiveness when resistance is known to be a problem. The commonly prescribed formulation called Augmentin is a combination of the -lactamase inhibitor shown below with amoxicillin (shown above). It is used to treat childhood ear infections when resistance is suspected, and many kids know it as the white liquid that tastes like bananas. Which of the statements below are true statements? 1. The stereochemistry of the fusion between the four-and five-membered rings in the inhibitor and amoxicillin are different. 2. The inhibitor possesses enol ether and allylic alcohol functional groups while the antibiotic possesses a phenol and a secondary amide functional group. 3. Neither the inhibitor nor the antibiotic contains strained rings. 4. Both 1 and 2 are true.
2. How might the compound shown below work as a mechanism-based inhibitor of phosphoglucomutase? Use structural drawings to explain your answer. CI s=0 OH НО ОН
Describe how the following function as drugs: (a) AZT (b) cisplatin (c) daunomycin
An enzyme catalyzes the hydrolysis of an ester with a certain activity, but this activity is lost in a 3 M urea solution. What is the most likely explanation for the loss of activity? (A) Urea binds to the active site of the enzyme competitively with the substrate. (B) Urea causes the cleavage of the peptide bonds in the enzyme. (C) Urea causes the enzyme to denature and lose its specific three-dimensional shape. (D) Urea reacts with disulfide bonds in the enzyme.
A4 Your enzyme is inhibited by one of the compounds depicted above. The inhibitor for your specific protein is indicated via the PDB protein code shown.On the basis of the enzyme’s structure, its substrate and mechanism of action, predict what type of enzyme inhibition ( i.e., competitive or non-competitive) may occur and justify why you think this is the case . (Up to 50 words) TYPE NOT WRITE.
2. Which is a false statement regarding non-competitive enzyme inhibitor? (a) It binds to an allosteric site of the enzyme (b) It does not compete with the natural substrate for binding to the active site of the enzy (c) Its binding to the enzyme can induce a conformational change of the enzyme (d) It can be used in combination therapies with a competitive inhibitor (e) It usually is a mimic of the natural enzyme substrate 3. What is the purpose of structure-activity-relationship (SAR) studies? (a) To identify the drug target (b) To improve the pharmacokinetic properties of the drug (c) To determine which atoms or functional groups are important to the activity of a drug (d) To simplify the synthesis of the drug (e) To optimise activity of the drug
The activity of an enzyme requires a glutamic acid to display its -COOH functional group in the protonated state. Suppose the pK, of the -COOH group is 4.07. (a) Will the enzyme be more active at pH 3.5 or 4.5? Explain. (b) What fraction of the enzymes will be active at pH = 4.07? Explain. (c) At what pH will the enzyme show 78% of maximal activity?
Provide an electron pushing mechanism for the conversion shown below. Abbreviate the enzyme catalyst active site groups (BH* and B:) as needed. Which purine base is used? NH₂ Enz H₂O 'N NH
Selective serotonin reuptake inhibitors (SSRIs) are commonly prescribed antidepressants. SSRIs block the reabsorption of the neurotransmitter serotonin in the brain. Changing the balance of serotonin helps brain cells send and receive chemical messages, which in turn boosts mood. Two SSRI medications are Faverin (fluvoxamine, C15H21F3N2O2 ) and Zoloft (sertraline, C17H17Cl2N ). Determine the molar masses of Faverin and Zoloft
Other Guide Questions: 1. How is turnover number of an enzyme related to Vmax? 2. How can competitive and non-competitive inhibition be distinguished in terms of Km ? 3. Distinguish between the molecular mechanisms of competitive and non-competitive inhibition. 4. Why is a Lineweaver-Burk Plot useful in analyzing kinetic data from enzymatic reactions ? 5. What properties of metal ions make them useful cofactors? 6. Why necessary or advantageous for the body to make zymogens? 7. Briefly describe the role of nucleophilic catalysis in the mechanism of the chymotrypsin reaction. 8. Please make a derivation of the Michaelis-Menten equation.
3a. 3b. 3c 3d. 3e. CO₂ clavulanic acid CH₂-OH H Answer the following questions about clavulanic acid. Does clavulanic acid inhibit D-alanyl-D-alanine transpeptidase? Does clavulanic acid contain a ß-lactam? Does clavulanic acid contain a thiazolium ring? What is the result of the treatment of penicillinase with clavulanic acid? Does clavulanic acid form a covalent acyl-enzyme intermediate with penicillinase?
Which one will make the largest contribution to hydrophobic interactions via LDFs within the active site of an enzyme?