What enzyme uses phosphocreatine to make ATP? creatine kinase phosphorylation. oxidative What other ways can we make ATP? type your answer... phosphorylation and
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- Which of the answer choices is true about ATP synthase? Select all that apply. O ATP synthase makes a total of four ATP molecules in glycolysis. O ATP synthase is an important enzyme in the citric acid cycle. ATP synthase is an integral membrane protein. Under aerobic conditions, the F1 (globular) portion of ATP synthase catalyzes a catabolic reaction. V ATP synthase is a transport protein. O ATP synthase is an enzyme. ATP synthase relies on an electrochemical gradient of sodium ions to catalyze the formation of ATP.Watch this video and answer the question below https://youtu.be/AtlCxYDxY1I BCR-ABL is a kinase. A kinase is a type of enzyme that catalyzes the transfer of phosphate from one molecule to another. What are the substrates for the reaction that BCR-ABL catalyzes? Select all that are true.a- Substrate protein b- BCR-ABL c-ATP d- None of the listed molecules hereWhat's the difference between a calorie, an ATP molecule, and a GTP molecule? How does GTP become ATP? Also, explain how ATP is made. A clear explanation and graphic are required.
- Which is the correct link between conformation of the beta-subunit of the F1 component of the ATP synthase and ADP+P¡ or ATP? loose Binding Change Mechanism binding ATP ADP+P ATP Crepeat ADP ADP +P; ATP ATP +P; tight binding open ATP loose => binding ADP+Pi open => catalyzes ADP+P¡ into ATP tight => releases ATP open => releases ADP+P¡H+ passes through ATP Synthase actively. Group of answer choices False True No answer text provided. No answer text provided.What type of enzyme is responsible for initiating the process of glycolysis? Hydrolase. Dehydrogenase. Kinase. Phosphatase. Phosphorylase.
- In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP and glucose, forming a glucose-ATP-enzyme complex. The enzyme then transfers the phosphoryl group directly from ATP to glucose. Select the advantages of phosphoryl group transfer compared to hydrolysis and subsequent phosphorylation? Glucokinase increases the transition state energy, favoring glucose phosphorylation. Reaction intermediates do not need to be present in excess. The process takes advantage of the high phosphoryl group transfer potential of ATP. ATP hydrolysis is thermodynamically unfavorable compared to group transfer.What type of enzyme is responsible for initiating the process of glycolysis? O Hydrolase O Phosphorylase O Kinase O PhosphataseThe image below shows the ATP cycle. From the statements below, select the correct statement about the molecules X and Y involved in this process. (PO4 phosphorylation X X A 000 Y high energy phosphate bonds hydrolysis PO4 O In the ATP cycle, ATP (Y) is phosphorylated into ADP (X) O In the ATP cycle, ATP (X) is hydrolysed to form ADP (Y) O In the ATP cycle, ADP (Y) is converted to ATP (X) via a hydrolysis reaction In the ATP cycle, a phosphorylation reaction removes a phosphate unit from ADP (Y)
- Show your calculations for determining the number of ATPs that would be generated from the aerobic oxidation of the following triglyceride: H₂C H₂C -CH3Triglycerides can be broken down by hydrolysis reactions to glycerol and fatty acid chains in the digestive tract. Glycerol is easily converted to 1 phosphoglyceraldehyde also known as PGAL. Using your knowledge about how aerobic cellular respiration functions, explain how from this original glycerol molecule how many ATP’s are formed in this process. Make sure you include explanations where each ATP is made.Choose any/all that apply to the proton-motive force and ATP synthesis. The active pumping of protons through ATP synthase against their concentration gradient provides the energy needed for ATP synthesis. Rotation of the y subunit creates conformational changes in the active sites of ATP synthase that drive the release of ATP from the enzyme. Each 3 subunit of ATP synthase has a distinct amino acid sequence that accounts for the three different active sites present in the enzyme. The ATP molecules produced from the pair of electrons provided by NADH have greater potential energy than the ATP molecules produced from the pair of electrons provided by FADH₂. Inhibition of either ATP synthase or ATP translocase will stop flux through the electron- transport chain.