BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Question
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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Students have asked these similar questions
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? ____________________
If isolated regulatory subunits and catalytic subunits of ATCase are mixed, the native enzyme is reconstituted. What is the biological significance of the observation?
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
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
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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Similar questions
- 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 216KVal 190 Asp 189 Chymotrypsin Trypsin Elastasearrow_forwardB-lactamase is an enzyme found in many antibiotic-resistant bacteria that hydrolyzes and inactivates antibiotics like penicillin and cephalosporin. The amount of antibiotic hydrolyzed in 1 minute in a 10-ml solution containing purified ß-lactamase was measured as a function of antibiotic concentration. The kinetics of hydrolysis was performed for two antibiotic substrates (A and B). Assume that the concentration of ß-lactamase was kept constant during the assay. 12 Initial Velocity (nanomole/min) 10 8 2 0 10 20 | 30 [Antibiotic] (µm) 40 50 Antibiotic A Antibiotic B a) Based on the enzyme description, what type of enzyme is ß-lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Based on your answer in (a), what other reactant, in addition to the antibiotic substrate, needs to be in the active site of ß-lactamase for the hydrolysis reaction to proceed? c) From the reaction curves above, what is the approximate value of Vmax for the enzyme reaction? (Do not forget the…arrow_forward. The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAGarrow_forward
- Describe the features of the first binding site (for allosteric enzyme unprotkb-p39086), including structural features that recognize and complement the first ligand.arrow_forwardHow would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?arrow_forwardCatalytic residues are often found in loops between helices or strands for increased mobility duringcatalysis. Is the catalytic Cys predicted to be located in a loop between helices/strands?Are the other two catalytic residues, His and Asn, also found in loops?arrow_forward
- In a certain bacterial species, the amino acid arginine is synthesized by a particular enzyme so the bacterium does not require arginine in its growth medium. A key enzyme, which we will call arginine synthetase, is necessary for arginine biosynthesis. When these bacteria are given arginine in their growth media, they stop synthesizing arginine intracellularly. Based on this observation alone, propose three different regulatory mechanisms to explain why arginine biosynthesis ceases when arginine is added to the growth medium. To better understand the mechanism of regulation, you measure the amount of intracellular arginine synthetase protein when cells are grown in the presence and absence of arginine. Under both growth conditions, the amount of this protein is identical. Which mechanism of regulation would be consistent with this experimental observation?.arrow_forwardWill rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIarrow_forwardMost bacterial mutants that require isoleucine for growth also require valine.Why? Which enzyme or reaction would be defective in a mutant requiringonly isoleucine (not valine) for growth?arrow_forward
- Azaserine inhibits amidotransferases. State the purine precursor that resembles azaserine. Which step in the purine biosynthetic pathway will be inhibited?arrow_forwardSerine Proteases, such as chymotrypsin, contain Ser/Asp/His as a catalytic triad (i.e. three collaborating amino acids) of amino acids involved in enzyme catalysis. Why is this? Examine each amino acid of this catalytic triad (schematically detailed below: Ser195/Asp102/His57) and, based on your understanding of amino acid characteristics, predict what the role of each amino acid could be. His57 Ser195 Asp102arrow_forwardThe objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…arrow_forward
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