to degrade the peptidoglycan on the surface of bacterial cells.Initially the att
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to degrade the peptidoglycan on the surface of bacterial cells.Initially the attraction the peptidoglycan to nestle into the binding site of Lysozyme. Once between Hydrogen bonds allow to bound with its substrate, one in Lyso eclilitating a he key step in Lysozyme's mechanism of action is Glu 35 and Asp52 facilitating a hydroxyl group from between two ster to act as a strong nucleophile which cleaves and replaces the 21) The actvity of the hydroxyl group on the peptidoglycan is an example a. Binding energy b. Acid catalyzed reaction Covalent catalyzed reaction Metal ion catalyzed reaction d. 22) From the figure to the right, I can conclude/determine the following a. Km b. Vmax c. Presence of an inhibitor d. Typé of inhibitor e All of the above 23) it appears that lactate is a. b. c. An active enzyme A suitable substrate The reaction product An enzyme inhibitor An enzyme activator 24) The Vmax for the reaction with no lactate is b. 0.5 d. 12.5 C. 25) The Km for the reaction with 10mM lactate is d. 2.5 e - a. b. 0.5 C. 2 0.4 26) The fact that the Km is the same with 0, s, or 10 mM lactate indicates a. the reaction rate is not affected b. the binding affinity is not affected c. lactate does not affect the enzyme d. lactic acid is forming an acid base catalyzed reaction 27) draw the zwitterionic form of glycineExplanation / Answer
Hi,
21. Answer is Covalent catalyzed reaction
This is one of the 4 strategies used by enzymes to catalyze reactions. A nucleohilic attach happens on the substrate to break the bonds and form new covalent connections with the enzyme.
The binding energy is the energy which holds the nucleus together.
In metal catalyzed reaction, one of more metal ions such as Mg, Mn, Ca is involved.
Acid catalyze reactions occur between an acid and a base. A proton is transferred from an acid to base.
22. All the above
The intercept on the Y axis given value of Vmax. The negative intercept on X axis gives the Km. The three different lines passing through Y axis with different Vmax gives idea that inhibitors are used. All the three lines converge at X axis to give same Km but with different Vmax. This gives idea about the type of inhibitor.
23. An enzyme inhibitor
In the presence of lactate, the Y intercept in shifting up, this means the Vax is reducing. (The Y axis is 1/vmax, so when the intercept increases the value of Vmax deceases. But the X intercept i. e Km is unchanged. So this is a case of non competitive inhibitor.
24. The Y axis = 1/Vmax
When no lactate is present , the line cuts the Y axis at 0.5.
0.5 = 1/max
Vmax = 1/0.5 = 2
Answer is c.2
25. The Km intercept on X axis = -1/Km
so the value is = -0.4 = -1/km
Km = -1/(-0.4) = 2.5
26. b. binding affinity is not affected.
The lactate is not competing with the enzyme for substrate, as evident by unchanged Km, so it is only reducing the speed of the reaction.
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