BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
9th Edition
ISBN: 2818000069358
Author: BERG
Publisher: MAC HIGHER
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Chapter 10, Problem 43P
Interpretation Introduction
Interpretation:
The biological significance of the given observation that the native enzyme is reconstituted if isolated regulatory subunits and catalytic subunits of ATCase are mixed together is to be stated.
Concept introduction:
The enzyme which is able to do the conformational changes if an effector gets attached to it is known as allosteric enzyme. The small molecules that on binding to the enzyme regulate its activity are known as effectors. The effectors increases or decreases the activity of the enzyme.
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mTOR is a cytoplasmic kinase that regulates cell division. Its misregulation can lead to cancer. The canonical mTOR inhibitor, rapamycin, is FDA approved as a cancer treatment. Rapamycin is an allosteric inhibitor that does not bind anywhere near the substrate binding site of the enzyme.
A) What is the name of this type of inhibition?
B) Sketch a REPRESENTATIVE double-reciprocal/Lineweaver-Burke plot that includes the enzyme kinetics for BOTH the uninhibited and inhibited reaction. Be sure to:
1) Make ABSOLUTELY clear which curve is your uninhibited reaction and which is your inhibited reaction.
2) Label the X and Y axes.
3) Indicate what the X- and Y-intercepts represent with regards to Michaelis-Menten kinetics.
C) Can increasing the substrate concentration overcome this type of inhibition? Explain in a sentence or two.
a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? :
Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase
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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? ____________________
Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different
specificities.
(a) These proteases are considered serine proteases because the active sites contain serine, histidine
and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein
substrates.
(b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below.
Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala,
Arg, or Trp? Explain your answers.
Val 216
Val 190
Asp 189
Chymotrypsin
Trypsin
Elastase
Chapter 10 Solutions
BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41PCh. 10 - Prob. 42PCh. 10 - Prob. 43P
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