Use curve arrows to show the mechanism for the proposed conversion of 2a, 2b, 2c, and 2d to 4.
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- Explain the observation made when papase is added to the reaction catalyzed polyphenoloxidase?Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?CYP2E1 has a much higher Km for ethanol than ADH (11 mM versus 0.05 mM,respectively). When greater portions of ethanol are ingested (0.08% or 17 mM), which part of the statement would be true?
- You receive kinetic data for a transferase reaction where AX and B are substrates, while A and BX are products. You are asked to establish the reaction mechanism. Which graph will you draw first? A,B,C or D A. 1/Vo against [AXo] at different concentrations of [BXo] B. 1/[AXo] against 1/[Bo] at different concentrations of [BXo] C. 1/Vo against 1/[AXo] at different concentrations of [Bo] / D. 1/Vo against 1/[AXo] at different concentrations of [1/BXo]Write a balanced equation for the synthesis of TMP from dUMP that is coupled to the conversion of serine into glycine.This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
- . In Figure 6-11,a. in view of the position of HPA oxidase earlier in thepathway compared to that of HA oxidase, would youexpect people with tyrosinosis to show symptoms ofalkaptonuria?b. if a double mutant could be found, would you expecttyrosinosis to be epistatic to alkaptonuria?In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.Using the graph data I estimated Slope = 2.8, about the same as the steeper part of the maternal hemoglobin, does this represent a strong positive cooperativity between enzyme subunits?
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