9. Which of the following statements is/are correct for the shown reaction? A B CH₂-C²-3-CoA + Co 1 A. The reaction occurs in the mitochondria B. The small molecule in box a is GTP C. The reaction is a committed step for fatty acid catabolism D. The reaction requires biotin E. None of the above -CH₂-C-S-COA
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- Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?Decide whether each of the following statements is true about leucine transaminase. It's an enzyme, and leucine is its substrate. It speeds up the rate at which leucine is converted to other substances. It's a small molecule, with a molecular weight around 50 mol If you were to write a chemical equation for certain biochemical reactions of leucine, leucine transaminase would appear on both sides. Otrue Ofalse Otrue Ofalse Otrue Ofalse Otrue Ofalse X3. Answer the following questions about the metabolic pathway shown below: glutamate dehydrogenase e NH3 0-C-C-cH2-CH2-C- 0-C-CH-CH2-CH2-C-O + H,O + NAD + NH + NADH + H (a) Label the correct substances as the substrate, enzyme, and co-enzyme. (b) Which of the six classes does the enzyme of this reaction belong to? Why? (c) What is the name of the first molecule in this reaction? (d) Which metabolic pathway is this reaction likely to be a part of? A. glycolysis B. deamination C. beta-oxidation D. fermentation
- The aspartate carbamoylase (ATCase) is an enzyme that catalyzes the reaction below utilizing the multi-substrate reaction strategy which requires aspartate to bind first and then carbamoyl phosphate. As the reaction progresses product, Pi leaves before carbamoyl aspartate. aspartate NH3 O NH₂ carbamoyl phosphate O Ping pong O Double displacement O Random sequential O Controlled sequential O Ordered sequential ATCase P₁ NH₂ carbamoyl aspartateWhich class of enzymes catalyzes the following reactions? CH2- CH2- CH2 H2- C- CH2 AST CH2-C CH2 CH-NH + C=O + C=0 + CH-NH ČO0 Čo0 ČO0 ČO0" Aspartate Oxoglutarate Oxaloacetate Glutamate Select one: a. Oxidoreductase O b. Isomerase O c. Ligase d. Transferase8. The enzyme thiolase catalyzes one step in the ß-oxidation of saturated fats. One portion of the mechanism for this reaction is shown below. Describe the catalytic mechanism at work. (Note: "SCOA" is shorthand for the compound Acetyl-CoA) RCOCH₂COSCoA + HSCOA → H3C₂OSC0A + RCOSCOA HN NH CH₂ NH CH₂ CH₂ FS Grease NH3 H-SCO A NH CH2 CH₂ NH3 S Co A CH₂ NH 1 3 H-SCO A H3C SCO A NH3 a h-SCOA R-C S Co A CH₂ CH₂ C H₂ 0=0 HN NH + NH3 H₂C HN CH₂ NH CH₂ CH₂ 2 S Co A CH₂ NH NH
- 1. Outline the first round of lipid catabolism using a C18 saturated fatty acid. Indicate cofactors and type of chemistry that takes place. a. How much NADH, FADH2 and ACCOA are you getting from complete catabolism of this fatty acid? b. How many moles of ATP are you getting from the breakdown of this fatty acid? Keep in mind that in the mitochondria 1 mole FADH2 gives about 1.5 moles of ATP while 1 mole NADH yields about 2.5 moles of ATP.17. Omeprazole is a bioprecursor prodrug that is activated by protonation to give active metabolite that inhibits H¨,K*-ATPase covalently. By using chemical equations show activation of Omeprazole and its reaction to inhibit the H*,K*-ATPase. CH3 H3CO. s=0 H3C HNN Omeprazole OCH3 18. The following compound is an open-chain prodrug of benzodiazepines which undergo N- dealkylation to triazolam. Using chemical equations show transformation of this prodrug to triazolam. H3C H3C CH3 CH3 triazolam open-chain prodrug of triazolamThe enzyme that catalyzes reaction below can be classified as: CoO COO NAD+ NADH + H* Но- | malate -C- H-Ć- dehydrogenase Охaloacetate Malate isomerase lyase hydrolase oxidoreductase ligase transferase
- 1.The class of enzyme that catalyzes addition of a group to a double bond is? oxidoreductases lyases ligases isomerases hydrolases transferases 2. Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme? the active site of the enzyme must be rigid the active site of the enzyme must be flexible only one substrate could be converted to product by the enzyme the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures the entire enzyme must be rigid 3. Which of the following enzymes is found in blood serum and is diagnostic of prostate cancer if enzyme levels are elevated? alanine aminotransferase phosphohexose isomerase lactate dehydrogenase acid phosphatase alkaline phosphatase 4. A blood test returns elevated aspartate aminotransferase levels. You suspect that the patient has suffered a heart attack. What other serum enzyme level of…Consider the mechanism of enolase, as indicated below. Which of the following correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi- select question). Mg2+ Mg2 Enolase PO3- OH -C-C-H H OH HO H-N-H Lys 345 Glu211 2-Phosphoglycerate bound to enzyme Mg2+ Mg2 PO3- OH C-C-H OH HO H H-N*-H Lys 345 O Glu211 Enolic intermediate HOH PO3- H Phosphoenolpyruvate The metal ion (Mg2+) is helping to stabilize the extra negative charge that developed on the carboxyl group in the enolic intermediate. The metal ion (Mg2+) is serving as a general base, removing a proton in order to improve the quality of the nucleophile. The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through metal ion catalysis. The metal ion (Mg2+) is helping to orient the substrate properly in the active site. The metal ion (Mg2+) is accepting a proton in order to improve the quality of the leaving group.Consider the following reaction occurring at 298 K: OH CH₂OH OH -0. OH OH +ATP k₁ k₂ 0- OCH, OH OH 0 OH OH Glucose Glucose 6-phosphate Hexokinase is an enzyme that catalyzes this reaction. When the hexokinase is present the rate of k₁ is 1.3 X10-3 M-15-1 Calculate the activation energy for the hexokinase catalyzed forward reaction.. +ADP
