The synthesis of ATP from ADP and a P O is a catabolic reaction which stores energy for future cell use O is an exergonic (catabolic) reaction is an anabolic reaction which stores energy for later use O involves the hydrolysis (breaking) of a phosphate bond

What is the function of Histidine as part of the catalytic triad? O The alcohol group of histidine makes a nucleophilic attack on a peptide C=O bond. O The imidazole group acts as a general base and extracts a proton from serine activating it to attack the substrate O The imidazole group acts as a general base and extracts a proton from aspartate activating it to attack the substrate O The imidazole group acts as a general base and extracts a proton from aspartate allowing it to activate serine by transferring a proton

Under anerobic conditions how many ATP molecules will be produced when 3.5 moles of Glucose are being consumed?

synthesis of ATP has a positive delta G release a large amount of energy can be used to drive energetically unfavorable reaction None of the above

Which of the following regarding the ATP Synthase is INCORRECT? Protons flow through the a and c subunits The translocation of four protons through the ATP synthase fuels the synthesis of one ATP molecule The F1 domain can function as an ATPase The y subunit rotates while the xß dimers are stationary

In the Krebs cycle, the energy released by taking a compound off Coenzyme A is used to: Group of answer choices isomerize citrate decarboxylate isocitrate oxidize carbon make a new carbon-carbon bond. reduce carbon

Which of the following statements about the aerobic respiration of a molecule of glucose is FALSE? O It requires pathways and membrane complexes in both the cytosol and mitochondria in eukaryotes. O 34 molecules of ATP are generated by oxidative phosphorylation. O It requires pathways and membrane complexes in the cytosol and plasma membrane in prokaryotes. O It can generate 38 molecules of ATP in prokaryotes. O 12 molecules of ATP are generated by substrate-level phosphorylation.

the maximum amount of ATP that could be generated by the full oxidation of the compound ((CH3(CH2)4COOH 43 O 45 O 131 O 36 O 129 O

Many enzyme mechanisms involve transferring protons. Sidechains of an enzyme can act as catalytic acids or catalytic bases in this process. The figure below shows a step in the reaction by the enzyme triose phosphate isomerase. Glu165 group. -OH Would a catalytic acid gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic acid? co CH,OPO, 2- Activity remaining (%) Would a catalytic base gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic base? 100 Curve I 8 Glu¹65 9 Below are two pH rate profiles showing the percent activity as a function of pH. Answer the questions below about how these curves relate to the mechanism of triose phosphate isomerase. Remember what fraction of a titratable group is unprotonated at the pka. 10 OH In this reaction a carbonyl is converted into an enol intermediate. Circle the enol 100 Activity remaining (%) H Curve 2 CIOH CIOH CH₂OPO,²- 8 9 N N 10 7 pH PH i) Which of these curves shows the pH rate…

Which of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site