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Biochemistry Midterm 1 Review Questions 1. Allopurinol is called a suicide inhibitor of xanthine oxidase because: a.

the product of its oxidation is very strongly bound to the catalytic centre of the enzyme b. xanthine oxidase converts it to inactive compound c. it destroys the substrate molecules in the reaction mixture d. it increases affinity of xanthine to enzyme Allopurinol is a purine analog. It uses a form of irreversible enzyme inhibition (suicide inhibitor) that occurs when an enzyme binds a substrate analogue and forms an irreversible complex with it through a covalent bond during the "normal" catalysis reaction. The inhibitor binds to the active site where it is modified by the enzyme to produce a reactive group that reacts irreversibly to form a stable inhibitor-enzyme complex. 2. The rate of the reaction catalyzed by an allosteric enzyme at the given, very low, concentrate of a substrate ([S] << Km): a. does not depend on the concentration of an allosteric inhibitor b. does not depend on the concentration of an allosteric activator c. depends on both [S] and [allosteric activator] d. is described by the equation: Vo = (Vo*[S])/(Km + [S]) e. does not depend on pH and temperature 3. a. b. c. International unit (IU) of enzyme activity is defined as: number of reaction processes that each active site catalyzed per unit time specific activity of the given enzyme at 25 degrees C under optimal conditions activity of enzyme causing transformation of 1 micromole of substrate per minute at 25 degrees C under optimal conditions d. Kcat/Km paramet of the catalytic reaction e. Amount of micromoles of enzyme in 1ml of the solution 4. a. b. c. d. e. Value of Hill coefficient for allosteric proteins n<1 indicates on: odd number of subunits in protein molecule lack of cooperativity between ligand binding sites positive cooperativity between ligand binding sites negative cooperativity between ligand binding sites presence of covalent bonds between subunits of the protein

5. Km value for substrate X in the reaction catalyzed by enzyme E is 10^-4 M. You can expect that the reaction rate might be close to Vmax at substrate concentration: a. 10^-5 M b. 2*10^-5 M c. 10^-4 M d. 2*10^-4 M e. 10^-3 M

6. Cleavage of the peptide: asp-leu-val-tyr-ala-cys-arg-phe-thr-gly by chymotrypsin would form a smaller peptide that has an alanine at its amino terminus. Which amino acid would be at the carboxyl terminus of this smaller peptide? a. arg b. val c. phe d. gly e. glu f. asp 7. The charge of a protein of the following amino acid composition: Ala 20 Tyr 4 Cys 6 Lys 15 (+15) Val 10 Trp 3 Asn 12 His 11 (below pH of 6, His is protonated so has +1 charge) Leu 3 Gly 31 Asp 21 (-21) Ile 12 Pro 12 Gln 7 Met 2 Ser 13 Glu 16 (-16) Phe 5 Thr 17 Arg 7 (+7) At physiological pH (7.4) is: a. +5 b. -5 c. 0 d. -15 e. +10 8.