Campbell Biology In Focus
Campbell Biology In Focus
2nd Edition
ISBN: 9780134203072
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece
Publisher: PEARSON
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Chapter 14.1, Problem 1CC

MAKE CONNECTIONS In a research article about alkaptonuria published in 1902, Garrod suggested that humans inherit two “characters” (alleles) for a particular enzyme and that both parents must contribute a faulty version for the offspring to have the disorder. Today, would this disorder be called dominant or recessive? (See Concept 11.4.)

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5) The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences. al.H.colbe91srtihot wolsd sldu non lom i anolterineon mundillups betsmus 8880
1. Consider the three-dimensional model of the tertiary structure of an enzyme below. Amino acids involved in binding are shaded blue, and amino acids involved in catalysis are shaded red.   A. Suppose research has shown that amino acid 82 in the red shaded region is lysine, an amino acid with a positively-charged side chain. This lysine is critical for catalysis. Other studies have found that amino acids 12 and 62 in the blue region are both phenylalanine, an amino acid with a nonpolar side chain, and are critical for substrate binding.   These amino acids are relatively close in the active site but are separated by 20-70 amino acids in the primary structure. Using what you know about protein structure, explain how amino acids separated in the primary structure can come close together in the active site.   B.  Use this information and figure 4.2 in your book to answer the following questions: Do you think changing amino acid 82, lysine, an amino acid with a positively-charged side…
. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)

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