EBK BIOCHEMISTRY
6th Edition
ISBN: 8220102959286
Author: GRISHAM
Publisher: CENGAGE L
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Chapter 28, Problem 4P
Multiple Replication Forks in E. coli II On the basis of Figure 28.2, draw a simple diagram illustrating replication of the circular E. coli chromosome (a) at an early stage, (b) when one-third completed, (c) when two-thirds completed, and (d) when almost finished, assuming the initiation of replication at oriC has occurred only once. Then, draw a diagram showing the E. coli chromosome in problem 3 where the E. coli cell is dividing every 20 minutes.
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Chapter 28 Solutions
EBK BIOCHEMISTRY
Ch. 28 - Semiconservative or Conservative DNA Replication...Ch. 28 - The Enzymatic Activities of DNA Polymerase I (a)...Ch. 28 - Multiple Replication Forks in E. coli I Assuming...Ch. 28 - Multiple Replication Forks in E. coli II On the...Ch. 28 - Molecules of DNA Polymerase III per Cell vs....Ch. 28 - Number of Okazaki Fragments in E. coli and Human...Ch. 28 - The Roles of Helicases and Gyrases How do DNA...Ch. 28 - Human Genome Replication Rate Assume DNA...Ch. 28 - Heteroduplex DNA Formation in Recombination From...Ch. 28 - Homologous Recombination, Heteroduplex DNA, and...
Ch. 28 - Prob. 11PCh. 28 - Prob. 12PCh. 28 - Chemical Mutagenesis of DNA Bases Show the...Ch. 28 - Prob. 14PCh. 28 - Recombination in Immunoglobulin Genes If...Ch. 28 - Helicase Unwinding of the E. coli Chromosome...Ch. 28 - Prob. 17PCh. 28 - Functional Consequences of Y-Family DNA Polymerase...Ch. 28 - Figure 28.11 depicts the eukaryotic cell cycle....Ch. 28 - Figure 28.41 gives some examples of recombination...Ch. 28 - Prob. 21PCh. 28 - Prob. 22P
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- The pyruvate dehydrogenase complex catalyzes the oxidative decarboxylation of pyruvate to form acetyl CoA. E₁, E2, and E3 are abbreviations for the enzymes of the complex. Classify the enzyme names, prosthetic groups, and reactions as E1, E2, or E3. E₁ E2 Answer Bank E3 transfer of electrons to FAD and then to NAD+ transfer of acetyl group to coenzyme A formation of hydroxyethyl-TPP hydroxyethyl group transferred to lipoamide thiamine pyrophosphate (TPP) FAD lipoamide dihydrolipoyl transacetylase pyruvate dehydrogenase dihydrolipoyl dehydrogenasearrow_forwardPatients with pyruvate dehydrogenase deficiency show high levels of lactic acid in the blood. However, in some cases, treatment with dichloroacetate (DCA), which inhibits the kinase associated with the pyruvate dehydrogenase complex, lowers lactic acid levels. How does DCA act to stimulate pyruvate dehydrogenase activity? DCA activates pyruvate dehydrogenase kinase. DCA increases phosphorylation levels of pyruvate dehydrogenase. DCA inhibits pyruvate dehydrogenase kinase. ODCA activates pyruvate dehydrogenase phosphatase. What does this suggest about pyruvate dehydrogenase activity in patients who respond to DCA? The pyruvate dehydrogenase complex is active only when phosphorylated by the kinase. The pyruvate dehydrogenase complex is active only in the presence of the kinase. The pyruvate dehydrogenase complex is completely inactive. The pyruvate dehydrogenase complex displays some residual activity.arrow_forwardThe reduced coenzymes generated by the citric acid cycle donate electrons in a series of reactions called the electron-transport chain. The energy from the electron-transport chain is used for oxidative phosphorylation. Which compounds donate electrons to the electron- transport chain? H₂O NADH பப NAD+ ATP ADP FADH₂ FAD Which compounds are the final products of the electron-transport chain and oxidative phosphorylation? H₂O NADH NAD+ ΠΑΤΡ Π ADP FADH₂ FAD Which compound is the final electron acceptor in the electron-transport chain? Оно NADH NAD+ ATP ADP FADH₂ FADarrow_forward
- Hexokinase in red blood cells has a Michaelis constant (KM) of approximately 50 μM. Because life is hard enough as it is, let's assume that hexokinase displays Michaelis-Menten kinetics. What concentration of blood glucose yields an initial velocity (V) equal to 90% of the maximal velocity (Vmax)? [glucose] = What does the calculated substrate concentration at 90% Vmax tell you if normal blood glucose levels range between approximately 3.6 and 6.1 mM? Hexokinase operates near Vmax only when glucose levels are low. Hexokinase normally operates far below Vmax. Hexokinase operates near Vmax only when glucose levels are high. Hexokinase normally operates near Vmax mMarrow_forwardClassify each coenzyme or distinguishing characteristic based on whether it corresponds to catalytic or stoichiometric coenzymes. Catalytic coenzymes Answer Bank Stoichiometric coenzymes lipoic acid FAD used once coenzyme A regenerated thiamine pyrophosphate (TPP) NAD+arrow_forwardThe oxidation of malate by NAD+ to form oxaloacetate is a highly endergonic reaction under standard conditions. AG +29 kJ mol¹ (+7 kcal mol-¹) Malate + NAD+ oxaloacetate + NADH + H+ The reaction proceeds readily under physiological conditions. = Why does the reaction proceed readily as written under physiological conditions? The NADH produced during glycolysis drives the reaction in the direction of malate oxidation. The steady-state concentrations of the products are low compared with those of the substrates. The reaction is pushed forward by the energetically favorable oxidation of fumarate to malate. Endergonic reactions such as this occur spontaneously without the input of free energy. Assuming an [NAD+ ]/[NADH] ratio of 8, a temperature of 25°C, and a pH of 7, what is the lowest [malate]/[oxaloacetate] ratio at which oxaloacetate can be formed from malate? [malate] [oxaloacetate]arrow_forward
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