5. Enzymes are incredibly effective at facilitating chemical reactions and must be controlled- or the chemical reaction won't stop and the reactant(s) might be used up. (A) Use 3 different colors to color the coding circles and corresponding structures in the figures. (B) Draw an arrow pointing to the active site in each figure. (C) Beneath each diagram, write the type of inhibition and briefly, in your own words, explain what is happening. PG al JartW Mool bluow nolsoeen er edw gni nobisvitae ert wori gniworla en qsp/ru to can't S uid can't weib (A) wole Ts w.bind b (8) bris bobl ewm bind oll omysne erlf yd beoue o.gons O Enzyme O Reactant (substrate) O Inhibitor Enzyme Enzyme Type of inhibition: Type of inhibition:

5. Enzymes are incredibly effective at facilitating chemical reactions and must be controlled- or the chemical reaction won't stop and the reactant(s) might be used up. (A) Use 3 different colors to color the coding circles and corresponding structures in the figures. (B) Draw an arrow pointing to the active site in each figure. (C) Beneath each diagram, write the type of inhibition and briefly, in your own words, explain what is happening. PG al JartW Mool bluow nolsoeen er edw gni nobisvitae ert wori gniworla en qsp/ru to can't S uid can't weib (A) wole Ts w.bind b (8) bris bobl ewm bind oll omysne erlf yd beoue o.gons O Enzyme O Reactant (substrate) O Inhibitor Enzyme Enzyme Type of inhibition: Type of inhibition:

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Q) Can a reversible enzyme be regulated by product inhibition? Justify your reasoning. (4 sentences MAX)
“Induced fit” means that when a substrate binds to an enzyme’s active site, (a) it fits perfectly, like a key in a lock (b) the substrate and enzyme undergo conformational changes (c) a site other than the active site undergoes aconformational change (d) the substrate and the enzyme become irreversibly bound to each other (e) c and d
3. Inside the treasure chest, you find that whoever last left this treasure had discovered an amazing new enzyme that will revolutionize life as we know it. It’s clear from the diagram provided along with the vial that the enzyme converts a substrate (S) into a product (P), with a Ks of 5 mM. You decide to set up an experiment: you add the enzyme to an initial substrate concentration of 15 µM. You note that after 8 minutes the concentration of the substrate is halved. What is the rate constant k, the vmax and the product concentration after 14 minutes?
C)|Myth: The specificity of an enzyme for its substrate is explained by the lock and key hypothesis. Fact: The lock and key hypothesis is outdated! What is our current model for understanding regarding how enzymes recognize and bind to substrates?
1. The enzyme you are studying uses the substrate pictured at right. An inhibitor box in the freezer contains two tubes labeled Inhibitor #1 and Inhibitor #2, along with the structures of the compounds contained within them and their respective Ki. Which one is more likely to be the non-competitive inhibitor? Inhibitor #1 K₁ = 10 μM m CH₂OH OH -0, $ OH OH Inhibitor #2 K₁ = 50 μM Briefly Justify: OH CH₂OH OH OH OH Substrate
2. “Most enzymes are gene-encoded proteins." Using this lens, explain: A) effects of increased temperature on the rate of enzymatic reactions, and B) effects of decreased temperature on enzymatic reactions, and C) importance of optimal pH and ionic strength on enzymatic reactions.
2. Draw a graph showing a downhill (spontaneous) reaction, that requires some activation energy to get it going. Then draw and clearly label on the graph b. The activation energy for the reaction (use a bracket to indicate the upper and lower limits) c. The free energy change for the reactions (use a bracket to indicate the upper and lower limits) d. How an enzyme will change the energetics of the reaction. I suggest you use a dotted line for the enzyme.
A) Myth: Enzymes are specific for one substrate. Fact: Like most enzymes, alliinase can act on multiple different substrates. Explain why most enzymes can act on more than one substrate compound. (Refer to the “Alliin-like Substrates" panel in your answer.)
4. An enzyme-substrate complex has a Kd = 100 nM. A competitive inhibitor with which of the following Ki values will be most effective at inhibiting this enzyme? A) K₁ = 10 nM B) K₁ = 100 nM C) K₁ = 1000 nM D) None of the above - only the KM is important Briefly explain:
20) Normally an enzyme has maximal enzyme activity at 37°C, but once it has been heated to 100°C and then cooled back down to 37°C the enzyme is no longer active. Why?
1. Describe the two ways by which the activity of an enzyme can be inhibited.
You are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?