A enzyme of the amino acid catabolism undergoes sequential displacement of substrates at its catalytic site. Which enzyme is it?
A enzyme of the amino acid catabolism undergoes sequential displacement of substrates at its catalytic site....
Suppose you are researching a special enzyme named "Generic Enzyme." Generic Enzyme has an amino acid side chain functional group that must be in the protonated form for the enzyme to be active. You have just purified Generic Enzyme and found that 1 in every 4 individual Generic Enzyme molecules is active. Your special Generic Enzyme is at a pH of 7.75. Generic enzyme has a phenolic hydroxyl group which is responsible for its catalytic activity. What is the pKa...
41. points) a) Draw the catalytic triad as it appears in the active site of any serine protease: b) The following hexapeptide was cut with trypsin. thr-val-glu-lys-his-gin Using the single letter amino acid code, write the sequence of the ping pong reaction in the boxes provided below. Enzyme -Enzyme Double-displacement reaction c) You mutate the S1 pocket of trypsin from Glutamate to Isoleucine. What are the two new products of the digestion of the hexapeptide in part b (still use...
Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site on the enzyme that is not the active site. 2. Insecticides and nerve gases act as irreversible inhibitors of nerve conduction. an enzyme needed for 3. A inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate. 4. Usually, an nhibitor forms a covalent bond with an amino acid side group within...
Enzyme 6. Where do substrates bind on an enzyme? A. allosteric site B. active site C. receptor D. ion channel 7. Enzymes are capable of increasing the rate of a chemical reaction through which of the following means? A. changing AG from positive to negative B. reducing the activation energy C. changing the equilibrium point of the reaction D. increasing kinetic energy 8. When a molecule can occupy the same active site as the substrate, a situation called can result...
There are several examples of human genetic disorders that affect amino acid catabolism. Three examples include, phenylketonuria, Argininemia, carbamoyl phosphate synthetase I deficiency. For each indicate the process that is defective in the disease condition, name the defective enzyme and list a few symptoms/effects.
1. The sequential mechanism for an enzyme, E, with two substrates, Si and S2 is shown below. Write the full rate equations for all species in the mechanism E+S ES ESI E S ESI S2 ESI S2 ESIS2 ESI S2 ki k. k2 k-2 k3 ESIS2 EP
The following questions are based on the papin mechanism below: Explain the role of each amino acid in the catalytic triad. Site directed mutagenesis replacing the active site asp in the papain protease with an ala showed that catalytic activity was not significantly affected. Why would you think that asp is not so critical in the cysteine proteases? Hi R CH2 NH-R oe 0 hole oxyanion hole 0 oxyanion hole CH a) Hi R CH2 NH-R oe 0 hole oxyanion...
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...
ginine is a glucogenic amino acid. Catabolism of arginine yields alpha-ketoglutarate, a citric acid cycle intermediate and glucogenic precursor. The enzymes and steps of the catabolism of arginine are shown below. Place the correct structure in each target, starting with arginine.
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...