Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 9, Problem 11RQ
What property enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated?
- They are polar.
- They are non-polar.
- They contain a hydroxyl group.
- They occur more frequently in the amino acid sequence of signaling proteins.
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Students have asked these similar questions
The following diagram shows and enzyme (in gray) that has transiently bound cyclic AMP, a signaling molecule (in
salmon pink). What kind of bonds/associations are the amino acid side chains in the enzyme (green, blue) forming
with the cyclic AMP? Focus only on the bonds/associations indicated by the black arrows.
serine
CH2
N-H
cyclic AMP
/ (CH2)3
`NH
`c=NH,
`NH2
serine
arginine
N
CH
-Hio
threonine
CH2
glutamic
acid
CH2
(B)
covalent bonds
hydrogen bonds
van der Waals forces
hydrophobic forces
ionic bonds
O O O O O
d) Alcohols usually don't behave as a weak acids, but tyrosine does. Explain why Y
ionizes, while S and T do not.
e) Is Y ionization physiologically relevant? Explain.
f)
Y is capable of being phosphorylated by kinases in vivo. What mutation might
you introduce to render Y unphosphorylatable? Constitutively phosphorylated?
Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two
glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein,
the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the
glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3)
bond also to three sialic acid residues, then also O-linked to the glycoprotein.
The saccharide was cleaved from its sialic acid residues. The treatments and results are as
follows:
1. hydrolysis by B(1-> 4) - disaccharide products
2. hydrolysis by a(1-> 4) - release of 2 disaccharide & 2 monosaccharide units.
Show the structure of the saccharide.
Chapter 9 Solutions
Biology 2e
Ch. 9 - Figure 9.8 HER2 is a receptor tyrosine kinase. In...Ch. 9 - Figure 9.10 In certain cancers, the GTPase...Ch. 9 - Figure 9.17 Which of the following statements...Ch. 9 - Figure 9.18 What advantage might biofilm...Ch. 9 - What property prevents the ligands of cell-surface...Ch. 9 - The secretion of hormones by the pituitary gland...Ch. 9 - Why are ion channels necessary to transport ions...Ch. 9 - Endocrine signals are transmitted more slowly than...Ch. 9 - A scientist notices that when she adds a small,...Ch. 9 - Where do DAG and IP3 originate? They are formed by...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. Function of 1st glycoprotein – glucose transporter protein Function of 2nd glycoprotein – Na*-K* receptor/ transporter Why is there a difference in the functions of the two glycoproteins?arrow_forwardDiisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195. Which statement is true of DIPF's inhibitory mechanism? DIPF randomly modifies all serine residues on the protein, and if enough is added, the serine in the active site will eventually be modified. DIPF approaches serine 195 more closely than other substrates. DIPF looks like the substrate for chymotrypsin and binds in the active site as a competitive inhibitor. Serine 195 is in an environment that gives it a higher than normal reactivity with respect to DIPF.arrow_forwardSH2 domains bind phosphotyrosine residues in deep pockets on their surfaces. Would you expect SH2 domains to bind phosphoserine and phosphothreonine with high affinity? Why or why not?arrow_forward
- H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14arrow_forwardSynthesis of peptide bonds is [exorgonic or endergonic]. Thus in isolation, this reaction would [occur or not occur] in cells. Peptide synthesis at the ribosome is coupled to GTP hydrolysis which is an [exergonic or endergonic] process thus making the overall process of synthesizing peptides [spontaneous or not spontaneous].arrow_forwardSnake venom contains many hydrolase enzymes, including several serine proteases. One such protease (present in high concentrations in snake venom) mimics the action of thrombin to activate fibrin. The venom protease cleaves peptide bonds with a specificity for basic, positively charged amino acids. This enzyme is incubated with a substrate peptide with the sequence SNPDCKVALYMTW. Draw a mechanism for the peptide hydrolysis of this specific peptide catalyzed by this snake venom protease. Include the structure of the active site amino acids of the enzyme and the substrate peptide group (including the full structure of the 2 specific amino acids that contribute to the scissile peptide group in the substrate) in your mechanism. Use the curved arrow convention to illustrate the flow of electrons.arrow_forward
- Consider, for example, that a particular serine residue is phosphorylated to activate the protein. In the lab, a similar effect is achieved by mutating this residue to either a D (aspartic acid) or E (glutamic acid). What could be the reason?arrow_forwardWhat amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?arrow_forwardYou have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme's inactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by the absence of the S1 binding pocket. replacement of serine 195 with a positively charged residue. presence of a positively charged residue in the S1 binding pocket. presence of a negatively charged residue in the S1 binding pocket.arrow_forward
- TPCK is a molecule with large hydrophobic groups. Why does TPCK inactivate chymotrypsin but not trypsin? TPCK looks like the substrate for chymotrypsin, but not trypsin, and thus can bind in its active site and modify His-57. Trypsin does not have a His residue present in the active site to react with TPCK. TPCK is a transition state analog for chymotrypsin, but not trypsin. TPCK binds to trypsin but does not modify its active site.arrow_forwardTrypsin cleaves proteins on the carboxyl side of lysine. Trypsin inhibitor has a lysine residue, and binds to trypsin, yet it is not a substrate. Explain.arrow_forwardReceptor tyrosine kinases such as the epidermal growth factor (EGF) receptor can basically be broken down into three domains: (1) An extracellular, ligand binding domain, (2) A transmembrane domain that must cross through the cell membrane, and (3) an intracellular domain. Match the amino acid with the domain that it would MOST LIKELY be associated with. Lysine (choose (1), (2), or (3) from above) A tyrosine residue capable of being phosphorylated on its hydroxyl group (choose (1), (2), or (3) from above) Isoleucine (choose (1), (2), or (3) from above)arrow_forward
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