Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Question
Chapter 6, Problem 20RQ
Summary Introduction
To review:
The reason for the inherent specificity of enzymes to react with one stereoisomeric form of the substrate and convert into the product.
Introduction:
The enzyme specificity is referred to as the property of the enzyme to bind to a single type of substrate. The stereoisomeric forms are the ones in which two molecules are made of the same atoms and have the same sequence of bonded atoms. They differ only in the arrangement of the atoms, thereby changing the three-dimensional conformation.
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A carboxypeptidase is a metalloenyme (its active site contains one or more metal
ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the
terminal amino acid of a polypeptide chain (where the free carboxyl group occurs).
The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the
enzyme is represented in the scheme below:
Glu
Zn++
COO™
OH
H3C
CH₂
HC
NH
IO C
H
H
Poche apolaire
-H
H
O+N: C N
H
H
H
NH₂
Arg 145
Туг 248
NB: This scheme gives a planar representation of the spatial structure of the active
site where indicated contacts (hatched lines) are supposed to occur in the 3D
structure of the enzyme.
1- Describe the interactions that occur between the ligand and amino acid residues
of the active site.
2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the
following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L-
tyrosine.
The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses (sugars with six carbons). The hexokinases will bind only D-hexose sugars and not their L-counterparts. In general terms, describe the features of enzyme structure that make this specificity possible.
When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 6 - Prob. 1QCh. 6 - Prob. 2QCh. 6 - Prob. 3QCh. 6 - Prob. 4QCh. 6 - Prob. 5QCh. 6 - Prob. 6QCh. 6 - Prob. 7QCh. 6 - Prob. 8QCh. 6 - Prob. 9QCh. 6 - Prob. 1RQ
Ch. 6 - Prob. 2RQCh. 6 - Prob. 3RQCh. 6 - Prob. 4RQCh. 6 - Prob. 5RQCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQCh. 6 - Prob. 8RQCh. 6 - Prob. 9RQCh. 6 - Prob. 10RQCh. 6 - Prob. 11RQCh. 6 - Prob. 12RQCh. 6 - Prob. 13RQCh. 6 - Prob. 14RQCh. 6 - Prob. 15RQCh. 6 - Prob. 16RQCh. 6 - Prob. 17RQCh. 6 - Prob. 18RQCh. 6 - Prob. 19RQCh. 6 - Prob. 20RQCh. 6 - Prob. 21RQCh. 6 - Prob. 22RQCh. 6 - Prob. 23RQCh. 6 - Prob. 24RQCh. 6 - Prob. 25RQCh. 6 - Prob. 26RQCh. 6 - Prob. 27RQCh. 6 - Prob. 28RQCh. 6 - Prob. 29RQCh. 6 - Prob. 30RQCh. 6 - Prob. 31RQCh. 6 - Prob. 32RQCh. 6 - Prob. 33RQCh. 6 - Prob. 34RQCh. 6 - Prob. 35RQCh. 6 - Prob. 36RQCh. 6 - Prob. 37RQCh. 6 - Prob. 38RQCh. 6 - Prob. 39RQCh. 6 - Prob. 40RQCh. 6 - Prob. 41RQCh. 6 - Prob. 42RQCh. 6 - Prob. 43FBCh. 6 - Prob. 44FBCh. 6 - Prob. 45FBCh. 6 - Prob. 46FBCh. 6 - Prob. 47FBCh. 6 - Prob. 48FBCh. 6 - Prob. 49FBCh. 6 - Prob. 50FBCh. 6 - Prob. 51FBCh. 6 - Prob. 52FBCh. 6 - Prob. 53SACh. 6 - Prob. 54SACh. 6 - Prob. 55SACh. 6 - Prob. 56SACh. 6 - Prob. 57SACh. 6 - Prob. 58TQCh. 6 - Prob. 59TQCh. 6 - Prob. 60TQCh. 6 - Prob. 61TQCh. 6 - Prob. 62TQCh. 6 - Prob. 63TQCh. 6 - Prob. 64TQCh. 6 - Prob. 65TQCh. 6 - Prob. 66TQCh. 6 - Prob. 67TQCh. 6 - Prob. 68TQCh. 6 - Prob. 69TQCh. 6 - Prob. 70TQCh. 6 - Prob. 71TQCh. 6 - Prob. 72TQCh. 6 - Prob. 73TQCh. 6 - Prob. 74TQCh. 6 - Prob. 75TQCh. 6 - Prob. 76TQCh. 6 - Prob. 77TQCh. 6 - Prob. 78TQCh. 6 - Prob. 79TQCh. 6 - Prob. 80TQCh. 6 - Prob. 81TQ
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- A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…arrow_forwardWhat happens to a denatured enzyme regarding its functionality? How can that result be explained with the help of the lock and key model?arrow_forwardHow is it possible to determine the structure of an enzyme substrate complex by x ray crystallography when the reaction is over so quickly and the x ray analysis takes at least several minutes?arrow_forward
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