Be sure to solve all parts otherwise I will downvote 18. Which one of the following factors should be on the x-axis of the graph to accurately describeenzyme reaction rate?а. pHb. temperaturec. enzyme concentrationd. substrate concentrationCH,19. The structure shown to the right is a (nucleic acid / nucleotideNHneither). It contains (ribose / deoxyribose / neither), and thenitrogenous base is a (purine / pyrimidine / neither).-o-CH2ÓH20. Write the nucleotide sequence of the RNA formed from a segment of DNA, if the DNA templatestrand is: 5'- A CTGGA-3'.Be sure to indicate which is the 5' end and which is the 3' end21. Pyruvate can be converted into three possible products depending on the conditions and theorganism. Describe two of these products along with the conditions that lead to their formation.Reaction Rate

Enzymes are the biological catalysts that fasten the rate of chemical reactions. They are neither…

18. Which one of the following factors should be on the x-axis of the graph to accurately describe enzyme reaction rate? a. pH b. temperature c. enzyme concentration d. substrate concentration CH 19. The structure shown to the right is a (nucleic acid / nucleotide / neither). It contains (ribose / deoxyribose / neither), and the nitrogenous base is a (purine / pyrimidine / neither). NH. CH2 OH 20. Write the nucleotide sequence of the RNA formed from a segment of DNA, if the DNA template strand is: 5'- AC TGGA-3'. Be sure to indicate which is the 5' end and which is the 3' end 21. Pyruvate can be converted into three possible products depending on the conditions and the organism. Describe two of these products along with the conditions that lead to their formation. Reaction Rate

18. Which one of the following factors should be on the x-axis of the graph to accurately describe enzyme reaction rate? a. pH b. temperature c. enzyme concentration d. substrate concentration CH 19. The structure shown to the right is a (nucleic acid / nucleotide / neither). It contains (ribose / deoxyribose / neither), and the nitrogenous base is a (purine / pyrimidine / neither). NH. CH2 OH 20. Write the nucleotide sequence of the RNA formed from a segment of DNA, if the DNA template strand is: 5'- AC TGGA-3'. Be sure to indicate which is the 5' end and which is the 3' end 21. Pyruvate can be converted into three possible products depending on the conditions and the organism. Describe two of these products along with the conditions that lead to their formation. Reaction Rate

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...

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The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
The following data describe the catalysis of cleavage of peptide bonds in small peptides by a protease: Substrate K (1/s) K₁, (mM) k./K₁ (mM/s) A 0.1 10 B 1 1 10 0.1 100 0.02 8,000 0.05 10,000 0.5 Use this information to answer the next three questions. BODEF с D E F 0.01 1 100 5,000 160,000 20,000 4. Which substrate binds to the enzyme with the highest affinity? a. A b. B C. C d. D e. E f. F
Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH
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…
10) The graph shown below is the pre-steady state data for the serine protease (chymotrypsin) enzyme. Explain how this result suggests the formation of a covalent enzyme intermediate in the active site during the first step in the pathway. 3.0 2.0 1.0 1 3 Time (min) p-Nitrophenol (mol/mol of enzyme) 2.
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. F 1 M The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. 1 O Match the specificity pocket (identified by red number) to the residue that occupies it. 3 R Match the specificity pocket (identified by red number) to the residue that occupies it. 4 W 2 1. D 2. E 3. F 4. R 5. W 6. Y
When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
at punctures the bacterial cell wall has just been recently isolated from the F the peptide reveals the following information below: IOTE: when the sequence is nat knawn, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 °C Heptapeptide (2) Arg, Pro, Phe, Tyr, Ala, Lys 2.4-dinitrofluorobenzene DNP-Phe Lys and modified free Peptide 1 (Ala, Lys) amino acids Cleovoge with Trypsin, then chromatography Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Cleavage with Chymotrypsin, then chromatography Peptide 4 (Arg, Tyr) Peptide 5 (Lys, Pro, Ala, Arg) When answering the questions below, please use the ONE-LETTER CODE for the amino acid, with NO spaces and symbols between each letter. 1. What is the C-terminal residue? K 2. What is the N-terminal residue? F 3. What is the sequence of Peptide 3? GP 4. What is the sequence of Peptide 5? LPAA 5. What is the averall amino acid sequence? AL
1/Vo 1/[S] with I without I with I with I 1/vo without I *-*- 1/vo without I 1/[S] 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.
10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).