Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Question
Chapter 19, Problem 19.31AP
Interpretation Introduction
Interpretation:
The acidic and basic amino acid in the active site in the given diagram has to be determined.
Concept Introduction:
The enzyme can acts as a catalyst due to following capabilities given below:
- It can bring substrates and catalytic sites together.
- It gives acidic, basic or other groups required for catalysis.
- For the reaction to occur, enzyme holds substrate at exact distance and in exact orientation.
- It lowers the energy barrier.
Acidic amino acids: The amino acids which can donate
Basic amino acids: The amino acids which can accept
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
What type of intermolecular forces mainly exist between the side chains of each of the following pairs of amino acids? Select the single best answer for each part
below.
Note: Reference the Naturally-occurring amino acids table for additional information.
Part 1 of 3
Identify the following types of biomolecules and label and identify the functional groups
One or more of the compounds shown below will satisfy each of the following
statements. Not all compounds may be used; some may be used twice. Put the
number(s) in the blank.
(1) Found in chitin.
(2) An L-saccharide.
(3) The first residue attached to asparagine in N-linked glycans.
(4) A uronic acid.
(5) A ketose.
CH,OH
CoO
COO
OH
H
H
H
H
ОН Н
но
OH
OH H
OH H
HO
OH
H
NHC- CH,
Oso,
OH
(a)
(b)
(c)
CH,OH
CH,OH
CH,OH
C=0
CHOH
C=0
H-C- OH
CH,OH
но -с-н
ČH,OH
CH,OH
(d)
(e)
Chapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 19.1 - Prob. 19.1PCh. 19.1 - The enzyme LDH converts lactate to pyruvate. In...Ch. 19.2 - The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD,...Ch. 19.3 - Describe the reactions that you would expect these...Ch. 19.3 - Prob. 19.5PCh. 19.3 - Prob. 19.6PCh. 19.3 - Prob. 19.7PCh. 19.3 - Prob. 19.8PCh. 19.4 - Prob. 19.9KCPCh. 19.5 - Prob. 19.10KCP
Ch. 19.5 - Prob. 19.11PCh. 19.5 - Prob. 19.12PCh. 19.6 - Prob. 19.13PCh. 19.6 - Prob. 19.14PCh. 19.7 - (a) L-Threonine is converted to L-isoleucine in a...Ch. 19.8 - AZT (zidovudine) inhibits the synthesis of the HIV...Ch. 19.8 - Prob. 19.3CIAPCh. 19.8 - Prob. 19.16PCh. 19.9 - Does the enzyme described in each of the following...Ch. 19.9 - Prob. 19.18PCh. 19.9 - Compare the structures of vitamin A and vitamin C....Ch. 19.9 - Prob. 19.20PCh. 19.9 - Prob. 19.21KCPCh. 19.9 - Prob. 19.22PCh. 19.9 - Prob. 19.4CIAPCh. 19.9 - Prob. 19.6CIAPCh. 19.9 - Prob. 19.7CIAPCh. 19.9 - Enzyme levels in blood are often elevated in...Ch. 19.9 - Prob. 19.9CIAPCh. 19.9 - Prob. 19.23PCh. 19 - Prob. 19.24UKCCh. 19 - Prob. 19.25UKCCh. 19 - Prob. 19.26UKCCh. 19 - Prob. 19.27UKCCh. 19 - Prob. 19.28APCh. 19 - Explain how the following mechanisms regulate...Ch. 19 - Prob. 19.30APCh. 19 - Prob. 19.31APCh. 19 - Prob. 19.32APCh. 19 - Prob. 19.33APCh. 19 - Prob. 19.34APCh. 19 - Prob. 19.35APCh. 19 - Prob. 19.36APCh. 19 - Prob. 19.37APCh. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - What features of enzymes make them so specific in...Ch. 19 - Describe in general terms how enzymes act as...Ch. 19 - Prob. 19.42APCh. 19 - Prob. 19.43APCh. 19 - Prob. 19.44APCh. 19 - Prob. 19.45APCh. 19 - Prob. 19.46APCh. 19 - Prob. 19.47APCh. 19 - What is the difference between the lock-and-key...Ch. 19 - Why is the induced-fit model a more likely model...Ch. 19 - Prob. 19.50APCh. 19 - Prob. 19.51APCh. 19 - How do you explain the observation that pepsin, a...Ch. 19 - Prob. 19.53APCh. 19 - Prob. 19.54APCh. 19 - Prob. 19.55APCh. 19 - Prob. 19.56APCh. 19 - Prob. 19.57APCh. 19 - The text discusses three forms of enzyme...Ch. 19 - Prob. 19.59APCh. 19 - Prob. 19.60APCh. 19 - Prob. 19.62APCh. 19 - Prob. 19.63APCh. 19 - The meat tenderizer used in cooking is primarily...Ch. 19 - Prob. 19.65APCh. 19 - Why do allosteric enzymes have two types of...Ch. 19 - Prob. 19.67APCh. 19 - Prob. 19.68APCh. 19 - Prob. 19.69APCh. 19 - Prob. 19.70APCh. 19 - Prob. 19.71APCh. 19 - Prob. 19.72APCh. 19 - Prob. 19.73APCh. 19 - Prob. 19.74APCh. 19 - Prob. 19.75APCh. 19 - Prob. 19.76APCh. 19 - Prob. 19.77APCh. 19 - Prob. 19.78APCh. 19 - Prob. 19.79APCh. 19 - Prob. 19.80CPCh. 19 - Prob. 19.81CPCh. 19 - Prob. 19.82CPCh. 19 - Prob. 19.83CPCh. 19 - Prob. 19.84CPCh. 19 - Prob. 19.85CPCh. 19 - Prob. 19.86CPCh. 19 - Prob. 19.87CPCh. 19 - Prob. 19.88GPCh. 19 - The ability to change a selected amino acid...Ch. 19 - Prob. 19.90GPCh. 19 - Prob. 19.91GP
Knowledge Booster
Similar questions
- a) This molecule is produced when what amino acid is transaminated? b) What are the one- and three-letter abbreviations for this amino acid?arrow_forwardA pentapeptide has a titration curve that shows five inflection points for five equivalents of hydroxide added. How many residues have ionizable groups within their side chains (R-groups) based on this information?arrow_forwardIdentify the conjugate acid-base pairs in the following reactions: HNO2(aq) + H2O(l) → NO2 – (aq) + H3O+(aq) _______ ______ _________ ________ CH3NH2 + H2O(l) → CH3NH3+ + OH – _______ ________ ________ _________arrow_forward
- Draw the structure of the a-keto acid formed by removal of the amino group during the catabolism of leucine. Note: Reference the Naturally-occurring amino acids table for additional information. Click and drag to start drawing a structure. xarrow_forwardNote:- Provide detailed explanation for the reaction that involves the removal of nitrogen from an alpha-amino acid, forming an alpha-keto acid. Please explain with the help of an example.arrow_forwardFor each of the following pairs of amino acids, identify the strongest type of intermolecular forces involved when the side chains interact. Explain in terms of the chemical structures of the amino acid side chains. Use the following list: disulfide bridge, hydrogen bonding, hydrophobic interaction, or salt bridge. a) D and H b) C and C c) L and A d) G and S e) N and Tarrow_forward
- Many bioactive compounds are derived from amino acids. This compound, found in trace amounts in mammalian brains and hypothesized to play a role as a neuromodulator or neurotransmitter, is derived from an amino acid through removal of the backbone carboxylic acid group. The amino acid from which it is derived must be: (Write out the entire name; Spelling matters, but case does not; Do not include L- or D- in the name; For acidic amino acids write the full name, e.g. “so-and-so acid”)arrow_forwardDraw the generalized structure of an amino acid and label the functional groups:arrow_forwardDraw the tripeptide val-glu-his as it exists under physiological pH. Write the reaction for the hydrolysis of this tripeptide into the individual amino acids. Be sure to show the reaction conditions and the final products that result under these conditions.arrow_forward
- Glycine hydrochloride (Cl− H3N+CH2COOH) is a diprotic acid that contains a carboxylic acid group and an ammonium group and is therefore called an amino acid. It is often used in biochemical buffers. Solve, In analogy with Figure , sketch the titration curve of this diprotic acid.arrow_forwardDraw the zwitterion for each of the following amino acids: glycine threonine glutamic acid phenylalaninearrow_forwardTwo of the 20 common amino acids have two chiral carbon atoms in their structures. Identify these amino acids and their chiral carbon atoms.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. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals 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 LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals 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