Enzymes - exercise - Vladimíra Kvasnicová
Each question of the test contains 4 statements (a, b, c, d). You can obtain 1 point (correct answer), –1 point (incorrect answer) or 0 point (if ? is marked). All four statements can be either correct or incorrect or some of the statements can be correct and some incorrect. Use the following schema to complete the answer table: Y = I agree with the statementN = I disagree with the statement ? = I don't know NoNo abcd 1YN?YN?YN?YN? 2YN?YN?YN?YN? 3YN?YN?YN?YN? 4YN?YN?YN?YN? 5YN?YN?YN?YN?
NoNo abcd 1YN?YN?YN?YN? 2YN?YN?YN?YN? 3YN?YN?YN?YN? 4YN?YN?YN?YN? 5YN?YN?YN?YN?
Phosphatase catalyzes a) insertion of P i into a substrate b) removing of P i from a substrate c) hydrolysis of an ester bond d) reaction producing ATP
Phosphatase catalyzes a) insertion of P i into a substrate b) removing of P i from a substrate c) hydrolysis of an ester bond d) reaction producing ATP NoNo abcd 1YN?YN?YN?YN?
The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley ‑ Liss, Inc., New York, ISBN 0 ‑ 471 ‑ ‑ 2 dephosphorylation phosphorylation (hydrolytic cleavage of an ester bond) (isertion of phosphate to a substrate) hydrolase phosphotransferase (esterase)
Choose correct statements: a)dehydrogenases catalyze oxidative- reducing reactions b)carboxylases need ATP for their function c)kinases transfer a phosphate from an energy rich compound to a substrate d)hydroxylases catalyze oxidation of a substrate
Choose correct statements: a)dehydrogenases catalyze oxidative- reducing reactions b)carboxylases need ATP for their function c)kinases transfer a phosphate from an energy rich compound to a substrate d)hydroxylases catalyze oxidation of a substrate
The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley ‑ Liss, Inc., New York, ISBN 0 ‑ 471 ‑ ‑ 2 Alcohol dehydrogenase oxidation of a substrate without direct presence of oxygen (NAD + used as a coenzyme)
Carboxylase elongates a molecule by 1 carbon (as carboxyl, COO - ). It needs CO 2 disolved in water = HCO 3 -. It is a ligase – it needs energy for its function: ATP is cleaved to ADP and phosphate.
The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley ‑ Liss, Inc., New York, ISBN 0 ‑ 471 ‑ ‑ 2 Reaction catalyzed by glucokinase (or hexokinase)
The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley ‑ Liss, Inc., New York, ISBN 0 ‑ 471 ‑ ‑ 2 Hydroxylase = monoxygenase catalyzes an introduction of 1 oxygen atom to a substrate as –OH; the second oxygen (from molecular O 2 ) is reduced to H 2 O
Alanin aminotransferase (ALT) catalyzes a reaction of Ala with - ketoglutarate. The reaction produces a) oxaloacetate b) aspartate c) glutamate d) pyruvate
Alanin aminotransferase (ALT) catalyzes a reaction of Ala with -ketoglutarate. The reaction produces a) oxaloacetate b) aspartate c) glutamate d) pyruvate
The figure was adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley ‑ Liss, Inc., New York, ISBN 0 ‑ 471 ‑ ‑ 2 Alanine aminotransferase transfers –NH 2 group from alanine to -ketoglutarate (alanine is converted to pyruvate, -ketoglutarate gives glutamate) - reversible reaction -
Enzyme catalyzing cleavage of a bond between 2 amino acids in proteins belongs among a) lyases b) peptidases c) hydrolases d) transferases
Enzyme catalyzing cleavage of a bond between 2 amino acids in proteins belongs among a) lyases b) peptidases c) hydrolases d) transferases
The figure is found at (Jan 2007) H2OH2O AA 1 AA 2 dipeptide peptide bond
Choose a corret statement(s): a)maximal velocity V max is related to maximal number of substrate molecules transformed by the enzyme per unit of time b)K M is expressed in velocity units (mol.s -1 ) c)K M = concentration of a substrate needed to reach ½ V max of the reaction d)K M = concentration of a substrate needed for transformation of ½ enzyme molecules to complex enzyme-substrate
Choose a corret statement(s): a)maximal velocity V max is related to maximal number of substrate molecules transformed by the enzyme per unit of time b)K M is expressed in velocity units (mol.s -1 ) c)K M = concentration of a substrate needed to reach ½ V max of the reaction d)K M = concentration of a substrate needed for transformation of ½ enzyme molecules to complex enzyme-substrate
The figure is found at (Dec 2006)
K M of a pair enzyme-substrate a)is decreased by a competitive inhibitor b)is equal to the concentration of a substrate when an activity of the enzyme is maximal c)is increased by a noncompetitive inhibitor d)is directly proportional to an affinity of the enzyme to its substrate
K M of a pair enzyme-substrate a)is decreased by a competitive inhibitor b)is equal to the concentration of a substrate when an activity of the enzyme is maximal c)is increased by a noncompetitive inhibitor d)is directly proportional to an affinity of the enzyme to its substrate
The figure is found at (Dec 2006) Summary of an enzyme inhibition
The figure is found at (Dec 2006) K m describes affinity of an enzyme to its substrate ! indirect proportionality !
Choose a correct statement(s): a)an inhibition is competitive if an inhibitor competes with a substrate to be bound into an active site of an enzyme b)a noncompetitive inhibition can be decreased by an increasing of a substrate concentration c)competitive inhibitors have very often a similar structure as a substrate d)noncompetitive inhibitors decrease V max
Choose a correct statement(s): a)an inhibition is competitive if an inhibitor competes with a substrate to be bound into an active site of an enzyme b)a noncompetitive inhibition can be decreased by an increasing of a substrate concentration c)competitive inhibitors have very often a similar structure as a substrate d)noncompetitive inhibitors decrease V max
The figure is found at 13/05jpeg/05_jpeg_HTML/index.htm (Dec 2006) 13/05jpeg/05_jpeg_HTML/index.htm Inhibition of enzymes
Competitive inhibition inhibitor resembles substrate it is bound to an active site but not converted by the enzyme increases K m ( affinity of enzyme to its S) if concentration of a substrate is increased the inhibition is decreased the inhibition is reversible The figure is found at: (December 2006)
inhibitor binds at a site other than the substrate-binding site inhibition is not reversed by increasing concentration of substrate (no K m change) V max is decreased (it is related to decreasing of active enzyme concentration) reversible only if the inhibitor is not bound by covalent bond The figure is found at: (December 2006) Noncompetitive inhibition
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 1
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 2
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 3
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 4
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 1
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 2
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 3
Choose the proper graph describing a)competitive inhibition b)noncompetitive inhibition c)inhibition by substrate excess d)allosteric enzyme 4
The figure is adopted from Devlin, T. M. (editor): Textbook of Biochemistry with Clinical Correlations, 4th ed. Wiley ‑ Liss, Inc., New York, ISBN 0 ‑ 471 ‑ ‑ 2 Allosteric enzyme: a) monomeric, b) oligomeric