Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 19, Problem 3P
Predict the effects of the following compounds on intracellular nucleoside triphosphate levels. For each answer, plot percent initial
a. Effect of thymidine on dNTP levels
b. Effect of trimethoprim on bacterial rNTP levels
c. Effect of fluorodeoxyuridine on dNTP levels
d. Effect of hydroxyurea on dNTP levels
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Chapter 19 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 19 - Prob. 1PCh. 19 - Prob. 2PCh. 19 - Predict the effects of the following compounds on...Ch. 19 - Prob. 4PCh. 19 - Prob. 5PCh. 19 - Prob. 6PCh. 19 - Prob. 7PCh. 19 - A classic way to isolate thymidylate...Ch. 19 - Prob. 9PCh. 19 - Prob. 10P
Ch. 19 - Prob. 11PCh. 19 - Prob. 12PCh. 19 - Prob. 13PCh. 19 - Prob. 14PCh. 19 - Prob. 15PCh. 19 - Prob. 16PCh. 19 - Prob. 17PCh. 19 - Prob. 18PCh. 19 - Prob. 19PCh. 19 - Prob. 20PCh. 19 - Prob. 21PCh. 19 - Prob. 22PCh. 19 - Prob. 23PCh. 19 - Prob. 24PCh. 19 - Prob. 25PCh. 19 - Prob. 26PCh. 19 - Prob. 27P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Explain the function of histidine 57 in the mechanism of chymotrypsin.arrow_forwardDescribe the mechanism of action of 1 cycle of the ubiquitin (Ub) ligase system. Describe how the E1, E2 and E3 ligases work to covalently link Ub to the target protein, including which uses an energy source (and how), and the operative amino acids on the enzymes, Ub and target proteinarrow_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_forward
- In the following scenarios, glucose is absent. Judging these systems as a whole, decide if B-galactosidase and permease are constitutive (always), unable (never), or inducible for each situation. Note, you must use the words inducible, unable, or constitutive. You should only have one answer per block. Please format your answer as a table and upload as a pdf or doc file B-galactosidase Permease |A) I POZYA I PΟΖΥΤΑ" B-galactosidase Permease B) IS ΡΟΖΥΤΑ I POCZYA B-galactosidase Permease С) I POZ'YA ΓΡΟΖΥΑ B-galactosidase Permease D) I PO̟ZYA ΡΟΖΥΤΑ B-galactosidase Permease E) I PΟΖΥΑ I POZ'YAarrow_forwardA child with coarse facies, corneal clouding, joint stiffness and mental retardation is found to have a Damage to this enzyme directly affects which of partial defect in N-acetylglucosaminotransferase. the following biochemical functions? A. Formation of polysomes B. Microtubule attachment to centrioles C. Synthesis of ribosomal RNA D. Targeting of enzymes for lysosomes E. Transport of sugars into mitochondriaarrow_forwardCTP synthetase catalyzes the glutamine-dependent conversion of UTP to CTP. The enzyme is allosterically inhibited by the product, CTP. Mammalian cells defective in this allosteric inhibition are found to have a complex phenotype: They require thymidine in the growth medium, they have unbalanced nucleotide pools, and they have an elevated spontaneous mutation rate. Explain the likely basis for these observations.arrow_forward
- Kinases are enzymes that transfer a phosphoryl group from a nucleosidetriphosphate. Which of the following are valid kinase-catalyzed reactions? (a) ADP + CMP → AMP + CDP. (b) AMP + ATP → 2 ADP.arrow_forward(Note: The alpha subunit of the heterotrimeric G-protein complex becomes activated upon activation of a GPCR. ) What is the mechanism used to turn off the alpha subunit ?arrow_forwardBriefly describe the induced-fit conformational change when hexokinase binds its substrate.arrow_forward
- The objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…arrow_forwardExplain how the pKa for histidine 57 is important to its role in the mechanism of chymotrypsin actionarrow_forwardExplain the regulatory processes of purine synthesis that would result in an increase in the concentration of GMP.arrow_forward
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