16. This figure from Foundations should look familiar. Which protein is shown here?A) AglycosidaseB) A G-proteinC) ChymotrypsinD) HexokinaseE) TrypsincatalytictriadSer 195His 57HGly 193N-HR ŅCaCBAsp 102R'17. What kind of enzymatic mechanism is shown in this figure from Foundations?A) Specific acid-base catalysis with His57 as the baseB) Specific acid-base catalysis with Ser195 as the baseC) General acid-base catalysis with Ser195 as the baseD) General acid-base catalysis with His57 as the baseE) Metal ion catalysisN-H

Every enzyme has its own active site where substrate molecules bind and undergo a chemical reaction.…

Answered: 16. This figure from Foundations should…

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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a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? : Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Transpeptidases have two substrates. From Figure 2A, what type of mechanism do they most likely adopt in processing the two substrates? sequential or ping-pong c) β-lactams inactivate transpeptidases by forming a covalent bond with the serine residue in the active site. Based on this description and Figure 2B caption, what type of inhibitor are β-lactams? _________________________________________ d) Based on the mechanism for lactamase shown in Figure 3, what type of enzyme is lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase e) Based on your answer in d, what other reactant, in addition to the antibiotic substrate, needs to be in the active site of lactamase for the hydrolysis reaction to proceed? ____________________
Hydrolysis of β-endorphin (a peptide containing 31 amino acid residues) produces the following amino acids: Tyr 1), Gly 3), Phe 2), Met, Thr 3), Ser 2), Lys 5), Gin 2), Pro, Leu 2), Val 2), Asn 2), Ala 2), lle, His, and Glu Treatment with carboxypeptidase liberates Gln. Treatment with DNFB liberates DNP-Tyr. Treatment with trypsin produces the following peptides: Lys, Gly—Gln, Asn—Ala—He—Val—Lys, Tyr—Gly—Gly—Phe—Met—Thr—Ser—Glu—Lys, Asn—Ala—His—Lys, Ser—Gln—Thr—Pro—Leu— Val—Thr—Leu—Phe—Lys Treatment with chymotrypsin produces the following peptides: Lys—Asn—Ala—He—Val—Lys—Asn—Ala—His—Lys—Lys—Gly—Gln Tyr—Gly—Gly—Phe Met—Thr—Ser—Glu—Lys—Ser—Gin—Thr—Pro—Leu—Val—Thr—Leu—Phe What is the primary sequence of β-endorphin?
Q1 a) What is the difference between non-competitive or allosteric modes of inhibition for the compounds acting upon the caspases studied. b) How many caspase isozymes are known in humans? c) What is the reaction catalyzed by a caspase enzyme?
In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…
You perform Michaelis-Menten kenetics on i) trypsin and ii) a mutant form of the same enzyme (a single amino acid has been changed). The specificity constant for the mutant was 10 times larger than for trypsin. a) Define the specificity constant and explain using this definition how a larger value might occur. b) Explain how, if at all, a non-competitive inhibitor of trypsin would affect the specificity constant.
a) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?
In what way(s) are Trypsin, Chymotrypsin, and Elastase different? (choose 1) a) They target different amino acid residues in proteins. b) They use different reaction mechanisms c) Both of the above d) Neither of the above
9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
An increase in PCO2 will result in which of the following? O a) An increased affinity between PO, and Hb, shifting the oxyhaemoglobin dissociation curve to the right b) An increased affinity between PO, and Hb, shifting the oxyhaemoglobin dissociation curve to the left O c) A decreased affinity between PO, and Hb, shifting the oxyhaemoglobin dissociation curve to the right O d) A decreased affinity between PO, and Hb, shifting the oxyhaemoglobin dissociation curve to the left
Which of the following glycolytic enzymes is NOT subject to regulation a) Hexokinase b) PFK-1 c) Both GAPDH and Triose phosphate isomerase (TPI) d) Triose Phosphate Isomerase (TPI) e) GAPDH
(a) What are the Vmax and Km (including units) for Tigerzyme? b) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Tar Heel? (c) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Blue Devil?
Deduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, Ser

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