What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a protein with 200 residues aftermRNA synthesis, starting from amino acids? Assume that the hydrolysis of PP; is equivalent to the hydrolysis of ATP forthis calculation.number of ATP molecules:number of GTP molecules:400800Incorrect

The polypeptide chin consists twenty naturally occurring amino acids that are linked together by…

Answered: What is the smallest number of…

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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ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate. Which of the following are true for the protein, ATP synthase? Select all apply A mutation of Asp61 to glutamic acid would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to alanine A mutation of Asp61 to alanine would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to glutamic acid The F1 subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis The FO subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis
The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATE
How can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/s
. Phosphatidylserine (PS) is considered to be an intermediate in the biosynthesis of phosphatidylethanolamine (PE) in E. coli, yet PS is not found in appreciable amounts among E. coli membrane phos- pholipids. Because PS must be present in the membrane to serve as an intermediate, how might you explain its failure to accumulate to a significant extent? What kinds of experiments could test your pro- posed explanation?
answer only question g
Concerning enzymatic activity, a larger Km value indicates a/an: Select one: O lower affinity for its substrate O inhibitory process O larger enzyme O larger Vmax O greater affinity for the substrate Which is the least common type of chemical bond? Select one: O Hydrogen O Peptide O Covalent O lonic O Disulphide D-gluconic acid is: Select one: O an integral membrane protein O a codon O an oxidized sugar O phosphorylated O a large lipid molecule
A transmembrane protein helps catalyze the transport of solute A from the INSIDE TO the OUTSIDE of a cell. The reaction can be represented by the reaction coordinate diagram below. It is possible to conclude that the concentration of A on the outside of the cell is than its concentration on the inside AND that it is_ to expect that the protein will at some point form a continuous path between th cytosol and the extracellular environment. A inside A outside reaction coordinate O lower; reasonable O higher; unreasonable O higher; reasonable free energy
In bacteria, isocitrate dehydrogenase is regulated by phosphorylation of a specific Ser residue in the enzyme active site. X-ray structures of the phosphorylated and the nonphosphorylated enzyme show no significant conformational differences. How does phosphorylation regulate isocitrate dehydrogenase activity? O The phosphoryl group sterically hinders the substrate. O The phosphorylation bears a negative charge, which repels the substrate. O The phosphoryl group attracts positively charged Ca2* cations, which block the active site on the enzyme. None of the above.
Which of the following statements are true about the relationships of [S], KM, and Vmax? (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.
If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? 0.125 mM 0.25 mM 0.50 mM 1.25 mM 5.0 mM
what does the Hexa protein domain depict? (in relation with tay sachs disease)
Which of the following are true when enzymes and substrate interact? kı E + S ● ES- -P k-1 the rate of the formation of ES = k1 [ES] the rate of the formation of the product = k2[ES] k1 [ES] = k-1 [ES] the rate of breakdown of ES to reform the enzyme and substrate = K-1[E][S] the rate of formation of ES = k1[E][S]

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