Q: Using the table below, differentiate the effect of two varying pH levels (as indicated by by the…
A: Enzymes are affected by changes in pH. The most favorable pH value - the point where the enzyme is…
Q: Inhibition type Reversibility, Examples of use in conditions Process diagram, features medical…
A: Enzymes are proteins that enhance the rate of a biochemical reaction. Enzymes are sensitive to the…
Q: in simple words differentiate non competitive and competitive inhibition.
A: Enzymes are proteins that act as biocatalysts. Enzymes catalyze the biochemical and chemical…
Q: A competitive inhibitor is one that ________.
A: The class of proteins that increase the rate of the reaction that occurs inside the living body…
Q: VO (mM/min), Minus Substrate, mM vO (mM/min), Plus Inhibitor Inhibitor 0.5 23.5 16.67 1 32.2 25.25…
A: The reciprocal of the given kinetic data is as follows: 1/[S] mM-1 1/V (min/mM) minus inhibitor…
Q: xplain what is meant by Optimum pH. Does pH lower than optimum pH denature the enzyme? How about pH…
A: Enzymes are biocatalysts that fasten the rate of chemical reactions. It decreases the activation…
Q: Give the name of the enzyme that we have studied this semester that catalyzes the most similar…
A: Coenzyme A (Co A) → -SH group present in coenzyme A is a thiol, it can react with -COOH to form…
Q: Which type of Enzymatic inhibition is commonly found in Pharma and why?
A: The inhibitors are the molecules that inhibit or decrease the activity of enzyme in catalyzing the…
Q: Show graphically the dependence of reaction velocity on substrate concentration for an enzyme that…
A: The reaction velocity or rate of reaction increases with increase with substrate concentration. When…
Q: What is the difference between primary plots and product inhibitor plots of enzymes.
A: Enzymes are the biomolecules that speed up the rate of a chemical reaction by binding with the…
Q: Name one advantage of a noncompetitive inhibitor as a potential drug compared with a competitive…
A: Enzymes are the biological catalysts that play an important role in the metabolic reactions…
Q: Define
A: Enzyme kinetic is a branch of Biochemistry. There are several factors that enzyme catalysis are…
Q: In the course of purifying an enzyme, a researcher performs a purification step that results in an…
A: An enzyme is a biocatlyst that increases the rate of overall reaction. Activity of enzyme is…
Q: Why is the transition-state analog not necessarily the same as a competitive inhibitor
A: Competitive inhibitor is the inhibitor having the similar shape as the substrate of the enzyme and…
Q: Penicillin is an example of what A. Competitive B. Noncompetitive type of enzyme inhibitor? C.…
A: Penicillium affects bacterial growth by inhibiting cell wall synthesis. It is an antibiotic that…
Q: A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for…
A: Lineweaver-Burk plot is also known as the double reciprocal plot. Plot between the reciprocal of…
Q: How can you distinguish between a competitive inhibitor and an uncompetitive inhibitor…
A: Competitive inhibitor- In competitive inhibitor, an inhibitor that resembles the normal substrate…
Q: Let's imagine I want to construct a competitive inhibitor for an enzyme one day. Should it be…
A: An enzyme's activity may be inhibited irreversibly or reversibly. The irreversible inhibitor binds…
Q: Define and contrast competitive and non-competitive inhibition.
A: The enzyme activity can be inhibited by the binding of small molecules or ions. The process by which…
Q: Three organisms were tested biochemically for their production of energy, and various compounds were…
A: Various organisms can be identified on the number of ATP produced according to the presence of…
Q: Why can we say that having a pure non- competitive inhibitor present is similar to just having less…
A: Enzymes are often regulated by feedback inhibition, allosteric regulation, competitive inhibition,…
Q: Essay: In your own words explain the following concept in not more than 5 sentences a. The lock and…
A: A. The lock and key model showing enzyme-substrate interaction. In which the substrate behave like…
Q: Given the active site diagram and reaction mechanism, indicate the mechanism of irreversible…
A: Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to a…
Q: Distinguish between Competitive and non-competitive inhibition.
A: Proteins known as enzymes serve as catalysts, accelerating chemical reactions without undergoing any…
Q: enzyme inhibition
A: The various process inn our body like digestion, respiration, energy production, etc requires the…
Q: Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of…
A: enzymes are proteins that are made up of amino acids. Enzymes contain active sites. These active…
Q: An Eadie-Hofstee plot is shown below for the different types of enzyme inhibition. Match the line…
A: Eadie-Hofstee diagram also called as Woolf-Eadie-Augustinsson-Hofstee or Eadie-Augustinsson plot is…
Q: You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered…
A: Lineweaver-Burk plot, also known as double-reciprocal plot, is the graph plotted for Lineweaver-Burk…
Q: Briefly describe 3 general catalytic mechanisms and 2 catalytic mechanisms of enzymes
A: The enzyme is proteins that help to speed up the biochemical reactions in our body. The enzyme works…
Q: A noncompetitive inhibition is best overcome (or reversed) by: A. Increasing [enzyme] B. Increasing…
A: Competitive inhibition is the process in which a chemical substance inhibits the effect of another…
Q: I’m reviewing Enzyme Inhibition and am having issues wrapping my head around non-competitive and…
A: In Enzyme inhibition the inhibitors are bind to the enzyme and suppress the activity of enzyme.
Q: Briefly describe 3 general catalytic mechanisms
A: Enzymes are biological catalysts that minimize the amount of activation energy needed for a process…
Q: How can we identify a competitive inhibitor?
A: Enzyme inhibitions are the mechanism of inhibiting the catalytic reactions of an enzyme by using…
Q: Describe the relationship between an enzyme active site, the enzymes substrate and competition by…
A: Introduction : Every enzyme has an active site. Through this active site enzymes can interact…
Q: The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor…
A: Enzymes are catalysts that enhance the rate of biochemical reactions.
Q: What are the optimal conditions for an enzyme(full answer)?
A: Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: Name any two industrially important enzymes
A: Enzymes are proteins that act as biological catalysts to accelerate the chemical reactions occurring…
Q: All enzymes have an optimal temperature at which they work as well as an optimal pH for their…
A: Enzymes are proteins that act as catalysts in biochemical reactions that specifically alter the rate…
Q: The Michaelis-Menten constant Km is O a. Dependent on the enzyme concentration b. Numerically equals…
A: Ans- The Michalis-Menton constant Km is the concentration of the substrate at which an enzyme…
Q: Parallel lines on a Lineweaver-Burk plot are diagnostic of— noncompetitive inhibition.…
A: The answer is option e The answer is uncompetitive inhibition
Q: Write the difference between compititive and non compititive enzyme inhibitors.
A: Enzyme inhibitors binds with the active sites of enzymes and reduces the compatibility of substrate…
Q: effect of the temperature and ph on amylase temperature explain what is the purpose of this lab,
A: Starch Plants perform photosynthesis in the presence of sunlight using water and carbon dioxide to…
Q: In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of…
A: Inhibitors bind to the enzyme and affect enzyme activity and they bind to it covalently and…
Q: What effect will competitive inhibitor have on the apparent Km of an enzyme for its substrate?
A: Enzymes are biological catalysts that help in catalyzing or speeding up biological reactions by…
Q: Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest…
A: Enzymes are biocatalyst that increases the speed of reaction by lowering the activation energy.…
Q: Sultanilamide is an antimicrobial drug that mimics the shape of an important substrate for a…
A: Enzymes are basically the essential part of biological processes. These usually are known to…
Q: What could be a suitable control for the Enzyme and Substrate Concentration experiment.
A: Other molecules can control the activity of enzymes by increasing or decreasing their activity.…
Q: Where do lines intersect on a Lineweaver-Burk plot showing competitive inhibition? Uncompetitive…
A: An enzyme is a catalyst that speeds up a chemical reaction in the cells. Enzymes are proteins that…
Q: Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a…
A: Enzymes are the biocatalyst that increases the rate of biochemical reactions. where its ability…
PLEASE HELP WITH THIS PRACTICE QUESTION, MY MAIN REFERENCE IS CAMPBELL BIOLOGY TEXT BOOK.....A LENGTHY AND DETAILED ANSWER WOULD BE APPRECIATED..
Step by step
Solved in 2 steps
- 1. What is the relative activity and the degree of inhibition caused by a competitive5 What are the cofactors are involved in redox reactions? selected all that apply: A) FAD B) CoA C)NAD+A reducing chemical reaction. reduces the compound to a simpler form adds an electron to the substrate removes a hydrogen atom from the substrate is a catabolic reaction
- In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.______ are always changed by participating in a reaction. a. Enzymes b. Cofactors c. Reactants d. CoenzymesWhich of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation
- An allosteric inhibitor does which of the following? Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding Binds to the active site and blocks it from binding substrate Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate Binds directly to the active site and mimics the substrate.When deprived of oxygen, yeast cells obtain energy by fermentation, producing carbon dioxide, ATP, and (a) acetyl CoA (b) ethyl alcohol (c) lactate (d) pyruvate (e) citrateWhich of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.
- Which of the following substances does not participate in the CalvinBenson cycle? a. ATP b. NADPH c. RuBP d. PGAL e. O2 f. CO21. An organism that has peroxidase and superoxide dismutase but lacks catalase is most likely an1. What are the differences classification of enzymes? List 5 classification of enzymes and cite their functions.