From the three figures below, indicate which represents best the catalytic pocket of trypsin, a serine protease, secreted by acinar pancreatic cells.C)A)A. Figure A.B.Figure B.ⒸC. Figure C.Asp 189B)Asp 189Val 190Val 216work ofVal 216Val 190

Serine proteases are the group of enzymes that cleaves the peptide bond in proteins, where Ser…

Answered: From the three figures below, indicate…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?
Some are unable to taste thiourea and PTC. DNA sequence results for these individuals show a normal predicted amino acid sequence for the TAS2R38 gene. Provide an explanation that can account for insensitivity to thiourea. (a) First assuming a mutation involving the TAS2R38 gene (b) Then assuming a mutation in a gene other than TAS2R38
Which of the following glycolytic enzymes is NOT subject to regulation a) Hexokinase b) PFK-1 c) Both GAPDH and Triose phosphate isomerase (TPI) d) Triose Phosphate Isomerase (TPI) e) GAPDH
For each of the following statements, indicate whether it is true or false. [Select] [Select] The LDL particles are internalized through the endocytic pathway. A mutation that impairs the association of the LDL receptor with adaptin would cause depletion of LDL in the blood. [Select] In the endosome, the LDL particle dissociates from the LDL receptor because the pH in the endosome is higher than that in the transport vesicle. [Select] A mutation that impairs the recruitment of the LDL receptor into clathrin-coated vesicles would cause a decrease in cellular cholesterol level.
On the right is a diagram of plasma concentration of three metabolites: glucose, B- hydroxybutyrate, and free fatty acid of an experimental animal over weeks of starvation. 4. (a) Label the lines with the names of the three metabolites. Yellow: Red: 10 20 30 40 Blue: Days of starvation (b) What factor in the plasma binds to and transports free fatty acid (c) Where was B-hydroxybutyrate produced? Why it is produced? What are the purposes of producing it (d) How B-hydroxybutyrate is used as fuel in extrahepatic cells? Write down the reactions, enzymes, and cofactors (No need to elaborate on the TCA cycle). (e) How many ATP molecules or equivalent are generated after complete oxidation of one molecule of B-hydroxybutyrate? Show your calculations. Hint: You need to consider ATP consumption for bypassed steps that may normally yield or consume AT Plasma concentration (mM)
(a) What are the Vmax and Km (including units) for Tigerzyme? b) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Tar Heel? (c) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Blue Devil?
An "AA" genotype at the ALOX5AP -4900 A>G locus acting in the 5-lipoxygenase pathway may increase risk of breast cancer when intake of which fatty acid is high? a) Stearic acid b) Eicosapentanoic acid c) Linoleic acid d) Alpha-linolenic acid
6. More enzyme activity.... A) Discuss how proteolytic cleavage is used to achieve tight control of the activity of digestive enzymes. B) If proteolytic cleavage leads to irreversible activation of digestive enzymes, how is the activity of digestive enzymes reduced when no longer needed? There were two ways presented this semester. C) We looked at three serine protease enzymes: elastase, chymotrypsin, and trypsin. All three enzymes cut peptide bonds using a similar catalytic mechanism. Explain why these are called serine proteases. D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?
You perform Michaelis-Menten kenetics on i) trypsin and ii) a mutant form of the same enzyme (a single amino acid has been changed). The specificity constant for the mutant was 10 times larger than for trypsin. a) Define the specificity constant and explain using this definition how a larger value might occur. b) Explain how, if at all, a non-competitive inhibitor of trypsin would affect the specificity constant.
In acute lymphoblastic leukemia, the cancerous white blood cells typically lack the enzyme asparagine synthetase. Why is the administration of asparaginase an eff ective therapy for this type of cancer?
Define the following terms: a. thiolytic cleavage b. ketogenesis c. ketone bodies d. α-oxidation e. ACC
Answer the following using the picture attached: A. How does pepsin differ from chymotrypsin in terms of its active site residues and mechanism? B. How do these changes permit pepsin to operate at such a low pH?

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