If the Glu at the active site of lysozyme were mutated into a Gln’ what effect...
In the polypeptide Thr-Gln-Glu-Thr-Ser-Ile-Tyr-Glu what is the N-terminal amino acid?
The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state (protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme.
The effect of pH on the activity of an enzyme was examined. At its active site, the enzyme has an Ionizable group that must be positively charged for substrate binding and catalysis to take place. The Ionizable group has a pk of 6.0. The substrate is negatively charged throughout the pH range of the experiment At what pH=9. the enzyme will be operating at answer is either Vmax, 1/2 Vmax or less than 1/2 Vmax (type in one of the...
24. The enzymatic activity of lysozyme is optimal at pH S.2 and decreases above and below this phH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu and Asp5?. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. What is the ionization state of each residue at the pH optimum of lysozyme? (1 Pt) a. vcan the ionization states of these two amino acid residues explain...
Question 12 What is the C-terminal amino acid residue in the following polypeptide? Met-Pro-Ser-His-Ile-Gly-Glu-Gln-Arg-Tyr
What indicates that an enzyme inhibitor binds at an allosteric site?a.) The inhibitor has no effect on kcat.b.) The inhibitor increases kcat.c.) The inhibitor decreases kcat.
a. What is the Km and Vmax for PFK1 when treated with OmM (represents control for enzymatic activity) or with 5mM AMP Show work on the graph draw lines for Vmax and Km. Control: Vmax (AMP), 0.32 0.28 0.2 Km 0.24 0.20 (s)-FTY20 (20LM): 0.18 Vmax 0.12 0.08 0.04 Km 0.00 Fructose-6-phosphate (mM) b. Fructose-6-phosphate is the substrate of the reaction. Based on answer in "a", what type of regulation occurs with and what site on PFK1 is AMP likely...
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
What would happen to the signaling pathway if the receptor were mutated? What about if the hormone was mutated?
1) What role does the active site lysine play in the mechanism of CO2 fixation in Rubisco? Hypothesize what effect the mutation of this lysine to arginine would have on the protein.