General, Organic, & Biological Chemistry
3rd Edition
ISBN: 9780073511245
Author: Janice Gorzynski Smith Dr.
Publisher: McGraw-Hill Education
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 21, Problem 21.90P
Interpretation Introduction
Interpretation:
The induced-fit model and lock-and-key model of enzyme specificity needs to be explained, using the given representations for substrate and an enzyme.
Concept introduction:
Enzymes are defined as a biological catalyst for various reactions in the living organisms. Enzymes are specific in nature and bind to specific substrate to catalyze any biochemical reaction. There are two models which will explain the specificity of enzyme namely; induced-fit model and lock-and-key model. The molecule that bound to the enzyme is known as substrate and that particular area where the substrate bound is known as active site of an enzyme.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionChapter 21 Solutions
General, Organic, & Biological Chemistry
Ch. 21.2 - In addition to the amino and carboxyl groups, what...Ch. 21.2 - Draw both enantiomers of each amino acid in...Ch. 21.2 - Prob. 21.3PCh. 21.3 - Draw the structure of the amino acid valine at...Ch. 21.3 - Identify the amino acid shown with all uncharged...Ch. 21.4 - Identify the N-terminal and C-terminal amino acid...Ch. 21.4 - Prob. 21.7PCh. 21.4 - Prob. 21.8PCh. 21.4 - Prob. 21.9PCh. 21.4 - Prob. 21.10P
Ch. 21.4 - Prob. 21.11PCh. 21.5 - Prob. 21.12PCh. 21.6 - Prob. 21.13PCh. 21.6 - Prob. 21.14PCh. 21.6 - Prob. 21.15PCh. 21.7 - Why is hemoglobin more water soluble than ...Ch. 21.8 - Prob. 21.17PCh. 21.8 - Prob. 21.18PCh. 21.9 - Prob. 21.19PCh. 21.9 - Prob. 21.20PCh. 21.9 - Prob. 21.21PCh. 21.9 - Prob. 21.22PCh. 21.10 - Prob. 21.23PCh. 21.10 - Prob. 21.24PCh. 21.10 - Prob. 21.25PCh. 21.10 - Prob. 21.26PCh. 21.10 - Prob. 21.27PCh. 21.10 - Prob. 21.28PCh. 21.10 - Prob. 21.29PCh. 21.11 - Prob. 21.30PCh. 21 - The amino acid alanine is a solid at room...Ch. 21 - Why is phenylalanine water soluble but...Ch. 21 - Draw the structure of a naturally occurring amino...Ch. 21 - Draw the structure of a naturally occurring amino...Ch. 21 - For each amino acid: [1] draw the L enantiomer in...Ch. 21 - For each amino acid: [1] draw the L enantiomer in...Ch. 21 - Draw both enantiomers of each amino acid and label...Ch. 21 - Which of the following Fischer projections...Ch. 21 - For each amino acid: [1] give the name; [2] give...Ch. 21 - For each amino acid: [1] give the name; [2] give...Ch. 21 - (a) Identify the amino acid shown with all...Ch. 21 - Prob. 21.42PCh. 21 - Prob. 21.43PCh. 21 - Draw the structure of the neutral, positively...Ch. 21 - Prob. 21.45PCh. 21 - Prob. 21.46PCh. 21 - (a) Draw the structure of the two possible...Ch. 21 - Prob. 21.48PCh. 21 - Prob. 21.49PCh. 21 - For each tripeptide: [1] draw the structure of the...Ch. 21 - Prob. 21.51PCh. 21 - For each tripeptide: [1] identify the amino acids...Ch. 21 - Prob. 21.53PCh. 21 - Prob. 21.54PCh. 21 - Prob. 21.55PCh. 21 - Prob. 21.56PCh. 21 - Prob. 21.57PCh. 21 - Prob. 21.58PCh. 21 - Prob. 21.59PCh. 21 - Prob. 21.60PCh. 21 - Prob. 21.61PCh. 21 - Prob. 21.62PCh. 21 - What type of intermolecular forces exist between...Ch. 21 - What type of interaction occur at each of the...Ch. 21 - Prob. 21.65PCh. 21 - Draw the structures of the amino acids tyrosine...Ch. 21 - Prob. 21.67PCh. 21 - Prob. 21.68PCh. 21 - Prob. 21.69PCh. 21 - Prob. 21.70PCh. 21 - Prob. 21.71PCh. 21 - Hydrogen bonding stabilizes both the secondary and...Ch. 21 - Prob. 21.73PCh. 21 - Prob. 21.74PCh. 21 - Prob. 21.75PCh. 21 - Prob. 21.76PCh. 21 - What class of enzyme catalyzes each of the...Ch. 21 - What class of enzyme catalyzes each of the...Ch. 21 - Prob. 21.79PCh. 21 - Prob. 21.80PCh. 21 - Prob. 21.81PCh. 21 - What kind of reaction is catalyzed by each of the...Ch. 21 - Prob. 21.83PCh. 21 - How will each of the following changes affect the...Ch. 21 - Prob. 21.85PCh. 21 - Prob. 21.86PCh. 21 - Prob. 21.87PCh. 21 - Prob. 21.88PCh. 21 - Prob. 21.89PCh. 21 - Prob. 21.90PCh. 21 - Prob. 21.91PCh. 21 - Prob. 21.92PCh. 21 - Why must vegetarian diets be carefully balanced?Ch. 21 - Prob. 21.94PCh. 21 - Sometimes an incision is cauterized (burned) to...Ch. 21 - Why is insulin administered by injection instead...Ch. 21 - Prob. 21.97PCh. 21 - The silk produced by a silkworm is a protein with...Ch. 21 - Explain the difference in the mechanism of action...Ch. 21 - Prob. 21.100PCh. 21 - Prob. 21.101CPCh. 21 - Suggest a reason for the following observation....
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- The process by which an enzyme acts on the substrate can be described by the: a. lock-and-key model. b. enzyme-and-substrate model. c. enzyme folding model. d. catalytic model.arrow_forwardWrite a brief description of the relationships among each of the following groups of terms or phrases. Answers to the Concept-Linking Exercises are given at the end of the chapter. Enzyme, enzyme substrate, active site, induced fit modelarrow_forwardDraw a graph that shows the effect of increasing substrate concentration on the rate of an enzyme-catalyzed reaction (at constant temperature, pH, and enzyme concentration).arrow_forward
- Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.arrow_forwardThe human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum valuearrow_forwardConsider the tripeptide tyrosylleucylisoleucine. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has an acidic side chain?arrow_forward
- Consider the tripeptide leucylvalyltryptophan. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has a basic side chain?arrow_forwardWhich is NOT a characteristic of proteins? a. They contain genetic information. b. They can act as hormones. c. They can catalyze chemical reactions. d. They act in cell membrane trafficking.arrow_forwardOnce cooked, egg whites remain in a solid form. However, egg whites that are beaten to form meringue will partially change back to a jellylike form if allowed to stand for a while. Explain these behaviors using the concept of reversible protein denaturation.arrow_forward
- For the tripeptide SerArgIle which amino acid residues a. are hydrophilic b. are hydrophobic c. possess polar neutral R groups d. participate in two amide linkagesarrow_forwardWhat is the general role of enzymes in the human body?arrow_forwardWhich of the following is not a characteristic of enzymes? a. They are macromolecules. b. They act on substances. c. They are phospholipids. d. They initiate and decelerate chemical reactions. e. They act as catalysts.arrow_forward
arrow_back_ios
arrow_forward_ios
Recommended textbooks for you
- Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage LearningWorld of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage LearningWorld of ChemistryChemistryISBN:9780618562763Author:Steven S. ZumdahlPublisher:Houghton Mifflin College Div
- General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage LearningOrganic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,Introductory Chemistry: An Active Learning Approa...ChemistryISBN:9781305079250Author:Mark S. Cracolice, Ed PetersPublisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
World of Chemistry, 3rd edition
Chemistry
ISBN:9781133109655
Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCoste
Publisher:Brooks / Cole / Cengage Learning
World of Chemistry
Chemistry
ISBN:9780618562763
Author:Steven S. Zumdahl
Publisher:Houghton Mifflin College Div
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
Introductory Chemistry: An Active Learning Approa...
Chemistry
ISBN:9781305079250
Author:Mark S. Cracolice, Ed Peters
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY