Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 8, Problem 16P
Interpretation Introduction
Interpretation:
The result of an enzyme having a greater binding energy for the substrate in comparison to the transition state is to be stated.
Concept introduction:
The
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true.
Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.
an inorganic ion. Such as metal ion, that improves the fit of an enzyme with its substrate is a(n)?
X Incorrect.
Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the
reaction? Choose all that are correct.
The enzyme increases the AG value.
The enzyme increases the rate of reaction.
The enzyme decreases the rate of reaction.
The enzyme decreases the AG value.
The enzyme raises the activation energy.
The enzyme lowers the activation energy.
Chapter 8 Solutions
Biochemistry
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- dits description. Each term can only be used once. ( Choose] [Choose) on induced fit the free energy of activation, or aclivation energy nds. substrates enzyme-substrate complex on enzyme active site d its description. Each term can only be used once. Chioie pimagepegarrow_forwardModified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The Michaelis-Menten Constant (Km) of an enzyme is equal to the enzyme concentration at which the initial velocity of the reaction is one half of maximum velocity (Vmax).arrow_forwardMultiple-Cholce Queations. Read each queation carefully and chooze the beat answer. Enzymes make reactiona go by the activation energy of the теаction. A. alower: ralaing B. fnater: lowering C. faster: raiaing D. alower: lowering What do you call the model which assumes a high degree of recemblance between the shape of the aubatrate & the geometry of the binding site on the enzyme? C. Induced Fit D. Lock and Key A. Van't Hofft B. Michelia-Menten Which of the following does not belong to the group? A. Hydrolasea B. Lipasea C. Lyases D. Transferases Which of the following is true about urease being a hydrolase enzyme? A. It catalyzea the degradation of uracil B. It catalyzes the synthesis C. It catalyzes the hydrolyale of urea D. It catalyzes the degradation of all amines of urea 5. Enzyme are classifed Into how many major groups and ayatematically named by how many numbera separated by dota? A. 4 groups and 6 numbera, гегресtively C. 4 groups and 4 numbera, respectively D. 5 groups and…arrow_forward
- In full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.arrow_forwardMETABOLIC PATHWAYS. Carefully analyze the diagram below. Complete the diagram below by providing the name of the pathway (in oblongs beside arrows), OR the product or the precursor (rectangles). Choose your answer from the terms provided below. Write the capital letters of your answer on the space provided. The same answer can be used more than once. starch sucrose lactose 19 20 18 glucose gly cogen glycogenoly sis 17 Urea 1 cycle glucose ribos 3 16 gluconeogenesis glycolysis some amino acids 4 lactic acid amino acid catabolism 15 13 11 6 fats 12 acety FCOA ketone bodi 14 fatty add synthesis A.glucose B.fructose TERM BANK P. glycolysis Q. glycogenolysis C. galactose R. lipolys is FAD NAD+ S. ketogenesis E. pyruvate T. B-oxidation F.NADPH U. Kreb's cycle G. FADH2 V. fermentation W. glycogenesis X. lipogenesis J. glycerol Y.hydrolysis Z. oxidation AB. pentose phosphate pathway N. cellulose XY, electron transport chain D. urea 10 8 H. NADH I. NH3 9. K. H20 L. CO2 АТР M. maltose O. fatty…arrow_forwardThe allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!arrow_forward
- Please ASA. Thanku. In the reaction Na + Cl à Na+ + Cl-, which component is said to become ‘oxidized’ and which is considered reduced? Na, Cl Cl, Cl Na, Na Cl, Naarrow_forwardI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4arrow_forwardHelp please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_forward
- Select all that apply. Which of the following are not properties of enzymes? not required to sustain the life of an organism sensitive to pH and temperature of their environment able to interact with all compounds or substrates large proteins with a special surface patternarrow_forwardMatch with the given reactionA. The reaction that is slowest in reacting with the enzymeB. The reaction that is fastest in reacting with the glucose oxidaseC. The reaction that is most fitted in the active site of the enzymearrow_forwardFor 100 words. What are the two essential requirements to effectively carry out metabolic work?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY