Enzymes work by lowering the energy of activation. O True O False QUESTION 10 loy moro than it stahilizes the strate compler
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- Which of the following statement is FALSE ? pKa values of active site residues can be shifted from typical pKa values Enzymes increase Keq Near attack complexes have reacting molecules close enough to form Va der Waals contacts The transition state contains at least one partial bond. QUESTION 12 The angle o in a peptide best describes: O the angle between the two peptide bonds O the angle between the alpha carbon (Ca) and the amide O the angle between the alpha carbon (Ca) and the carbonyl O the angle between the alpha carbon (Ca) and its side chain QUESTION 13 Investigating how protein subunits come together studies: super- secondary structure Click Save and Submit to save and submit. Click Save All Ansuers to save all anscers 7977 Mostly cloody-n f estion B I ut of question PF budy As you increase the amount of substrate in a reaction (while keeping the enzyme concentration the same): Select one: O A. The amount of products formed should decrease OB. The amount of products formed should remain the same OC. The amount of products formed should increase Clear my choice Mixing hydrogen peroxide with an enzyme different than catalase (such as lactase) should also result in the formation of products. Select one: O True O False The temperature at which an enzyme works best can differ from enzyme to enzyme. Select one: O True False B 7 OAn enzyme that catalyzes a reaction such as the one below is alan: || C-0 || C-0 C=0 С —о — Н I| Н-С—Н H- C H H isomerase O kinase O dehydratase O dehydrogenase O phosphorylase O - I
- What are the effects of different light colors in photosynthesis? Different light colors will change the rate of photosynthesis Light color does not affect photosynthesis Carbohydrates are metabolized by light Photosynthesis does not require lightnisms reguiale Part A Covalent modification O The product of a series of reactions acts as an inhibitor for an earlior reaction. O Hormones control the synthesis of enzymes A regulator binds to the enzyme at a site other than the active site. This binding changes the shape of the enzyme and alters the catalytic ability of the enzyme. An inhibitor binds reversibly to the enzymesubstrate complex, blocking the binding of the second substrate to the active site The activity of an enzyme is influenced by the addition or removal of a group that is covalently bonded to the enzyme. O An inhibilor forms covalent bonds to the active site, permanently blocking it Submit Reuest Answet P PearsonGiven the active site and reaction mechanism below, what is the mechanism of irreversible inhibition of the inhibitor provided? Active Site Reaction Mechanism Inhibitor `NH2. н Он SH OH- OH OH HO- NH „NH OH OH OH -Mg²+ Uncompetitive Affinity-based Transition state analog Non-specific Mechanism-based
- Covalent modification O The product of a series of reactions acts as an inhibitor for an earlier reaction O Hormones control the synthesis of enzymes A regulator binds to the enzyme at a site other than the active site. This binding chang shape of the enzyme and alters the catalytic ability of the enzyme, An inhibitor binds reversibly to the enzymesubstrate complex, blocking the binding of th second substrate to the active site. The activity of an enzyme is influenced by the addition or removal of a group that is cove bonded to the enzyme. An inhibitor forms covalent bonds to the active site. permanently blocking it.an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form CTrypsin, Chymotrypsin, and elastase dltel O Oxyanion holes O Specificity pockets chal Active site amino acid residues Reaction mechanisms QUESTION 2 Which of the following is not true of enzymes? O They lower the free energy of the transition state. O They may alter the mechanism of the reaction. O They may make a reaction more exergonic. O They may chemically interact with their substrates. QUESTION 3 What initiates the reaction catalyzed by Trypsin? Click Save and Submit to save and submit. Click Save All Answers to save all answers.
- The classic concept of bond strain is more correctly described in what way? Select the correct response: The transfer of electron from one chemical moiety to another results to decrease in steric hindrance. The chemical bonds of the substrate is distorted due to the presence of metal ions in the vicinity of the active site. The transition state makes better contact with the enzyme than the substrate due to stabilization effect of various moieties in the active site. The electron cloud of the substrate is polarized by more electronegative moieties in the active site.A type Il beta turn has what residue as one of the four residues that make up the turn? OAP O B. G C.I O D.A O E. Q Once a substrate is bound to the active site, there are a variety of mechanisms that aid in the cleavage and formation of bonds. Thesa incudn. OA General acid base catalysis by amino acid side chains which can act as proton donors and acceptors. OB. Metal ion catalysis where tightly bound metal ligands can participate in cataus. Oc covalent catalysis where the enzyme forms transient covalent bonds with reactants and these bonds are later broken O D.all of the above E. only A and C The Ramachandran plot describes the peptide conformation by illustrating the position of the dihedral angles that can rotate following. OA side-chain steric hindrance B. restrictions imposed by secondary structure OC. main-chain clashes from the bulky carbonyl oxygen or amide nitrogen with other main-chain atoms or side-chains O D. All of the above E. None of the aboveAllosteric Inhibitors ● are constructed of level of protein polypeptide chains (demonstrating on each polypeptide. structure) with an ● The enzyme moves back and forth between an active state and an inactive state ● If a substance binds to the allosteric site and puts the enzyme into the active state, that substance is called an ● If a substance binds to the allosteric site and puts the enzyme into the inactive state, that substance is called
