1) An enzyme is denatured when it loses its native conformation and its biological activity. Denaturation of enzyme occurs when they lose the quaternary structure, tertiary structure and secondary structure which is present in their native state, and therby losing their activity.
2) An enzyme considered a catalyst because it speeds up chemical reactions without being used up. They are the biological catalyst that bind to substrate and produce products.
3) An enzyme is considered specific because of its ability to recognize the shape of a particular molecule. Specificity is achieved by binding receptors with complementary shape, charge and polar characteristics to the substrates.
4) A cofactor such as vitamin, binds to an enzyme and plays a role in catalysis. Cofactors serve many purposes; for instance, metal ions can help in stabilizing nucleophilic species within the active site.
5) When properly aligned the enzyme and substrate form an enzyme sustrate complex. The binding is explained by both lock and theory model and induced fit model.
6) A substrate binds to an enzyme at the active site, where the reaction occurs. The catalytic site and binding site together comprise the enzyme's active site.
7) In a catalyzed reaction a reactant is often called a sustrate. substrate is the chemical in a chemical reaction, which is organic in nature and reacts with a reagent to generate a product.
If you cut a circular plasmid with enzyme A that shows 2 enzyme A (A1 and A2) marked with specific base pairs, is the 0 rest mark also considered as a band? If there is enzyme A1 and enzyme A2 on a plasmid, are there 2 bands or 3?
1-What are the factors that affect enzyme activity? 2-How the present of denaturation affecting enzyme activity? 3-Explain how the excess of H2O2inhibit the enzyme?
COST-LAB QUESTIONS: 1. What happens to enzyme activity as the enzyme concentration is increased? 2. Based on your results, what is the optimum pH for lactase? 3. Do all enzymes in the body have the same optimum pH? Why or why not? 4. What happens to enzyme activity as the substrate concentration is increased? Explain why this occurs.
2-In an enzyme-catalyzed reaction, the rate of the reaction depends on which of the following at very low substrate concentrations? Select one: Neither enzyme concentration nor substrate concentration Enzyme concentration but not substrate concentration Substrate concentration but not enzyme concentration Both substrate concentration and enzyme concentration
Problem 2: (Enzyme Kinetics) A competitive inhibitor I interferes with an enzyme-catalyzed reaction according to the mechanism: E+S →ES, rate constant = ki, ES → E+S, rate constant = k-1, ES → E+P, rate constant = k2, E + EI, rate constant = k3. EI → E + I, rate constant = k-3. Assuming that the concentrations of S and I are much larger than the total enzyme concentration, derive an expression for the initial rate of appearance of product,...
O Fraction of Enzyme bound to Inhibitor HIV enzyme named above New Drug 1 OHIV enzyme named above New Drug 2 . HIV enzyme named above AZT 0 0.5 3 3,5 1 1.5 2 2.5 Concentration of Compound (nM) a) Two new drugs were developed that interact with the enzyme. The following data was acquired on this drug. Please interpret this data and tell me what it likely means. b) No binding of drug 1 or 2 was observed without...
2. Complete enzymatic reactions Enzyme: ALT
1. what is the Vmax of the
enzyme described in the equation?
2. what is the Km of the enzyme described in the equation?
Use the equation below to answer the questions that follow. $=0.4 165 ) +0.008
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
Question 2: You have just discovered a new enzyme that catalyzes the degradation of cellulose to glucose. You hope to commercialize this enzyme ultimately to invent a process for biofuel manufacture. In order to determine how efficient the enzyme is and how fast the enzyme catalyzes the reaction, you have to perform some basic enzyme kinetics. Plot the following enzyme data for the enzyme catalyzed reaction and determine the Km and Vmax. Show your graph with correct units on the...