Homework Answers
1. a. quantum tunneling
Quantum tunneling is a means whereby a catalyst can lower the activation energy of a reaction.
2. a. binds substrates in a manner that facilitates the formation of a product
An enzyme acts as a catalyst in a reaction, by binding substrates in order to form products
3. c. involves amino acids that are brought into close proximity by extensive protein folding and may require a prosthetic group such as a metal ion
4. d. bond distortion, proton transfer, and electron transfer
bond distortion, proton transfer, and electron transfer are three mechanisms of substrate activation.
hapters 5 and 6: Bioenergetics/Enzymes apter 6, Question 10: Multiple-Choice , Part A The active site...
hapters 5 and 6: Bioenergetics/Enzymes apter 6, Question 10: Multiple-Choice , Part A The active site for many enzymes O usually depends on only one amino acid O contains amino acids that are contiguous to one another along the primary sequence of the protein may require a prosthetic group such as a metal ion. O involves amino acids that are brought into close proximity by extensive protein folding О involves amino acids that are brought into close proximity by extensive...
Which statement about enzyme catalyzed reactions is not true? a) enzymes form complexes with their substrates....
Which statement about enzyme catalyzed reactions is not true? a) enzymes form complexes with their substrates. b) enzymes lower the activation energy for chemical reactions. c) enzymes change the K eq for chemical reactions. d) many enzymes change shape slightly when substrate binds. e) reactions occur at the "active site" of enzymes, where a precise 3D orientation of amino acids is an important feature of catalysis.
#9 quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and ...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
1. Complete the following sentences Word bank: competitive, noncompetitive, allosteric site, oxaloacetate, active site, different from,...
1. Complete the following sentences Word bank: competitive, noncompetitive, allosteric site, oxaloacetate, active site, different from, similar to, succinate Oxaloacetate would be a reversible ______ inhibitor because the structure of oxaloacetate is ______ the structure of succinate, the substrate for the enzyme. As a _____ inhibitor, oxaloacetate would bind to the ______ of the enzyme. Increasing the concentration of _______, the substrate for the reaction, would reverse the effect of the _____ inhibitor. 2. Complete the following sentences The ______...
6) For the following statements concerning inhibition, use the answers (1 pts each) A) competitiv...
chem 103: biochem
need help with answering these questions!!!
6) For the following statements concerning inhibition, use the answers (1 pts each) A) competitive inhibition B) non-competitive C) irreversible and D) not an inhibition a) Which inhibition can be reversed by adding an excess of the substrate? b) In which inhibition does the inhibitor resemble the substrate? c) Inhibitor binds to enzyme at different site than substrate, but it can be removed. d) An example is ethanol as an antidote...
1 point Nicotinamide adenine dinucleotide (NAD+) is an essential cofactor for many metabolic reactions. Lack of...
1 point Nicotinamide adenine dinucleotide (NAD+) is an essential cofactor for many metabolic reactions. Lack of the precursor to NAD+, niacin, results in the human disease called pellagra, thus humans have evolved salvage pathways to breakdown and re-synthesize NAD+ when needed. Below is the chemical structure of NAD+. Enzymes catalyze reactions in parts of the protein called an active site. This portion of the protein forms favorable weak interactions with the substrate and stabilize the transition state, which is crucial...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
high and detecting one product at a time Question 77 The initial velocity of an enzyme...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
THIS IS BIOCHEMISTRY A peptide has a low pI value. Which of the following amino acids...
THIS IS BIOCHEMISTRY A peptide has a low pI value. Which of the following amino acids are likely to be present? Glycine Serine Valine Aspartic aci Arginine The R-groups of which of the following pairs of amino acids could participate in the formation of salt bridge electrostatic interaction? Alanine and valine Valine and lysine Lysine and glutamate Serine and isoleucine Asparagine and glutamine Which of the following interactions does NOT contribute to stabilizing tertiary structure? Hydrophobic interactions Electrostatic interations...
hapters 5 and 6: Bioenergetics/Enzymes apter 6, Question 10: Multiple-Choice , Part A The active site for many enzymes O usually depends on only one amino acid O contains amino acids that are contiguous to one another along the primary sequence of the protein may require a prosthetic group such as a metal ion. O involves amino acids that are brought into close proximity by extensive protein folding О involves amino acids that are brought into close proximity by extensive...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
chem 103: biochem
need help with answering these questions!!!
6) For the following statements concerning inhibition, use the answers (1 pts each) A) competitive inhibition B) non-competitive C) irreversible and D) not an inhibition a) Which inhibition can be reversed by adding an excess of the substrate? b) In which inhibition does the inhibitor resemble the substrate? c) Inhibitor binds to enzyme at different site than substrate, but it can be removed. d) An example is ethanol as an antidote...
1 point Nicotinamide adenine dinucleotide (NAD+) is an essential cofactor for many metabolic reactions. Lack of the precursor to NAD+, niacin, results in the human disease called pellagra, thus humans have evolved salvage pathways to breakdown and re-synthesize NAD+ when needed. Below is the chemical structure of NAD+. Enzymes catalyze reactions in parts of the protein called an active site. This portion of the protein forms favorable weak interactions with the substrate and stabilize the transition state, which is crucial...
Part A - Overview of enzyme structure and enzymatic reactions Enzymes are large globular proteins. Much of their three dimensional shape is the result of interactions between the R (variable) groups of their amino acids. The active site is the portion of the enzyme that will interact with the substrate the molecule that the enzyme acts upon. The nature and arrangement of amino acids in the active site make each enzyme specific to a substrate and to the reaction it...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
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