- 1) An enzyme that catalyzes the transformation of one substrate is characterized by the following specificity: a)absolute: b) relative; c) stereospecificity; d)allosteric: e) group. 2) Most food and microbial enzymes are destroyed at {}^circ C a) 15 b) 25 c) 37 d) 80 3) Regulation of enzyme activity cannot be carried out by: a) covalent chemical modification; b) formation of a substrate-substrate complex; c) allosteric regulation; d) partial proteolysis. 4) The division of enzymes into classes is based on: a) substrate structure b) structure of coenzymes c) structure of reaction products d) type of catalyzed reaction 5) The Michaelis-Menten equation. If for Enzyme "A" Vmax equals to 100mu mol/mL sec and Km equals to 2 mM, what is the velocity of the reaction when substrate "B"concentration equals to 20 mM?
- 6. In the district of 500000 population 10 persons affected by achondroplasia (autosomal dominant disease) live. Define a number of heterozygous carriers in the population.
- 4) The active site of an enzyme a) remains rigid and does not change shape. b) is found at the center of globular enzymes. c) is complementary to the rest of the molecule. d) contains amino acids without sidechains. e) None of the above choices are correct. 1) What Is the name glven to the unligue combination of amino beld residues lit in entryme molecule that ensures complementary Interaction with the robstrate and direct particlpation in the act of catalysis: a) active site. b) allosteric site: c) molecular site d) cofactor: e) coenzyme 2) What is the name of the polypeptide part of the enzyme: a) apoenzyme; b) Isoenzyme, c) coenzyme, d) holoentyme; e) prosthetic group 3) What is the name of the section of the enryme molecule to which effectors bind causing a decres or Increase in entymatic activity: a) active site, b) allosteric site c) catalytic site; d) cofactor; e) anchor area? 5) The Michaelis-Menten equation. The Km for the Enzyme "A" for the substrate "B" was determined be 300mu M. When the substrate "B"concentration was set to 160 uM, the initial rate of the reaction w found to be 65.0mu mol/(mLast s) What is Vmax for Enzyme "A" under these conditions?
- 1) An allosteric site Is: a) a unique sequence of amino acid residues; b) a regulatory center distant from the active center; c) cofactor; d) molecular site; e) coenzyme. 2) What is the non-protein part of the enzyme called: a) apoenzyme; b) coenzyme; c) holoenzyme; d) multienzyme; e) isoenzyme; 3) What model of interaction between enzyme and substrate was proposed by Fisher: a) "hands and gloves" b) "key and lock" (+) c) "boots and feet" d) "racks" e) "induced correspondence"? 4) The Michaelis constant is numerically equal to the concentration of the substrate at which the reaction rate is equal to: a) maximum; b) 1/2maximum c) 1/5maximum d) 1/10maximum 5) The Michaelis-Menten equation. What is the Vo/Vmax ratio when [S]=4Km
- 1) Isoenzymes are: a) Inactive forms of enzymes; b) multiple forms of the enzyme; c) multienzyme systems; d) enzyme precursors. 2) The speed of the enzymatic reaction depends on: a) enzyme concentration; b) molecular weight of the enzyme; c) molecular heterogeneity of the enzyme; d) molecular weight of the substrate. 3) Zymogen is: a) Enzyme poison b) Enzyme modulator c) Enzyme precursor d) Enzyme inhibitor 4) Non-competitive inhibition is the inhibition of an enzymatic reaction caused by the addition of an inhibitor: a) to the substrate; b) to the enzyme -substrate complex; c) to zymogen. d) there is no correct answer 8) The Michaelis-Menten equation. The Km for the Enzyme "A" for the substrate "B" was determined to be 500mu M. When the substrate "B"concentration was set to 180 juM, the initial rate of the reaction was found to be 45.0mu mol/(mLast s) What is Vmax for Enzyme "A" under these conditions?
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