Write down the composition of tears .which enzymes are present in tears? What is the role of enzyme. Explain in detail
Q: describe the mechanism of each class of inhibitor, including how they impact the effective…
A: There are mainly four types of inhibitors . Competitive inhibitor Non-competitive inhibitor…
Q: Occasionally the “delicate” nature of enzymes is referred to. Explain why this adjective is…
A: Enzymes are made up of proteins. They behave as catalysts in several biochemical reactions happening…
Q: Suggest a name for the enzyme that catalyzes the following reaction.
A: The given reaction involves the reaction of phenylalanine (Phe) amino acid with the α-ketoglutarate…
Q: Identify three enzymes found in the body, their likely location inside the body, and the pH at which…
A: Enzymes are biocatalyst that perform specific chemical reaction. They are proteinaceous in nature…
Q: (c) Discuss the mechanism of action of the enzyme chymotrypsin.
A: Chymotrypsin is a protease enzyme that aids in the digestion of proteins. Chymotrypsin is a protein…
Q: Given each set of information which may include common name(s) and the reaction catalyzed, you are…
A: Note : Hi ! Thank you for the question. We are authorized to answer three subparts at a time. Since…
Q: . Based on what you know about enzyme inhibition, classify the following examples as irreversible,…
A: “Since you have posted a question with multiple sub-parts, we will solve first three subparts for…
Q: What is tissue inhibitors of metalloproteinases (TIMPs) ? How does it play an important role ?
A: Contact inhibition is the process by which cells stop growing when they come into contact with each…
Q: Given each set of information which may include common name(s) and the reaction catalyzed, you are…
A: Enzymes have a common name that provides little information about the reaction catalyzed by…
Q: Give the systematic names and the first three digits in the E.C. classifications of the enzymes…
A: Enzymes are biocatalyst. They increase the speed of reaction by lowering the activation energy. A…
Q: (i) (iv) 3.0 2.5 2.0 1.5 1.0 0.5 0.3 (ii) (iii) Air 20°C 101525Pa Limin
A: Bioreactor: It consist of a vessel where biological reactions takes place through the transformation…
Q: With appropriate chemical structures, explain the mechanism (mode-of-action) of fluoroacetate…
A: Fluroacetate is a highly toxic susbstance. FA is present in plant species and there ingestion can…
Q: For each of the following examples, indicate whether the drug is acting on physical process,…
A: Drugs can act on the body through various processes, including physical, chemical, and enzymatic…
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: ENZYME/PATHWAY 1. phosphofructokinase-1 2. pyruvate dehydrogenase complex 3. Krebs cycle 4. lactic…
A: Introduction Phosphofructokinase 1(PFK1)is a kinase enzyme that phosphorylates fructose…
Q: In 2-page worth of words (around 500), discuss in depth the risks and hazards of CYCLAMATE in the…
A: Cyclamate is an artificial sweetener made of synthetic materials that is Thirty to Fifty times…
Q: Explain the phenomenon of "induced fit" using hexokinase as an example.
A: Hexokinase is an enzyme that phosphorylates six-carbon sugar to a hexose phosphate
Q: What is the application of enzymes in clinical setting?
A: Enzymes are the proteinous structure that helps in increasing the rate of metabolism. The function…
Q: NH HO-P-o Br, in H,O OH он ОН Ba(ОН),
A: ATP→cAMP(cyclic AMP) Adenosine triphosphate reacts with barium in presence of water or with barium…
Q: Describe the reactants and products of the following enzyme catalyzed reaction. Names of molecules…
A: Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: The nonprotein heme group sits in the active site of the hemoglobin enzyme. The heme group…
A: Haemoglobin is an allosteric protein. It means that the binding of oxygen to one of the subunits is…
Q: Regarding the physical condition (characteristics of the solution/environment) in which an enzyme…
A: Enzymes are large molecular weight proteins that catalyse biochemical reaction. An enzyme's…
Q: In 2-3 paragraphs (must be typed) explain: Discuss the regulation of cholesterol synthesis.
A: Cholesterol synthesis is a complex process that is tightly regulated by a variety of factors,…
Q: Although STATINs are the first line therapy for the treatment of hyperlipidemia, sometimes it fails…
A: Hyperlipidemia refers to a condition that is caused due to the increase in the level of low-density…
Q: a. How does an enzyme speed up the reaction of a substrate? b. After the products have formed, what…
A: Enzymes help in catalysis or speeding up most biological reactions. The majority of enzymes are…
Q: Background: In this experiment, the lab instructor created a catecholase enzyme solution using…
A: The experiment conducted aimed to investigate the activity of the catecholase enzyme extracted from…
Q: Explain biochemical role of potassium.
A: Potassium is an essential nutrient required by the human body. It plays an important function inside…
Q: Explain about contact inhibition.
A: Cell division is the process by which a parent cell divides into two or more daughter cells. Cell…
Step by step
Solved in 2 steps
- The catalytic activity of enzymes depends on the presence of appropriate environmental conditions. Pepsin is a digestive enzyme found in the stomach and facilitates the digestion of large proteins. If pepsin is removed from this acidic environment of the stomach and is instead placed in a more basic environment, it will cease to function. Describe the specific effect that a change in environmental pH will have on pepsin and explain how this change can lead to inhibition of its catalytic activity. Respond in 4 to 6 complete sentences.D. Describe the effect that each of the following changes would have on the rate of a biochemical reaction involving the substrate arginine and the enzyme arginase Decreasing the arginine concentration Increasing the temperature from its optimum value 10°C higher than this value Increasing the arginase concentration Increasing the pH by one unit from its optimum valueAn acidic environment is inhibitory to decarboxylase activity. True False
- The nonprotein heme group sits in the active site of the hemoglobin enzyme. The heme group facilitates the reaction of the enzyme and is required to be present for the reaction to occur. Select the best answer. Question options: Heme is an example of allosteric inhibition. Heme is an example of a product. Heme is an example of a noncompetitive inhibitor. Heme is an example of a cofactor Heme is an example of a competitive inhibitor.. Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.C. What types of inhibitors of this enzyme is shown below? [1]. D. What effect (increase, decrease, stay the same) does the inhibitor have on Vmax? E. What effect (increase, decrease, stay the same) does the inhibitor have on Km?
- ( please give in detail with diagram in 2 or 1.5 pages )Show the chemical reaction that takes place when Benedict's reagent (Cu2+) reacts with glucose (Indicate color change).Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
- The answer choices are highest, lowest, and intermediate absorption.Background: In this experiment, the lab instructor created a catecholase enzyme solution using white potatoes. The potato was the source of enzymes and cofactors in the experiment, as potatoes have sufficient amounts of catecholase and, therefore, cofactors for catecholase. A chilled potato had the peel removed by the instructor and then was chopped into pieces. The potato is peeled so that the brown skin does not interfere with the brown color of the benzoquinone. If this were to occur, the absorbance would seem higher due to the brown potato skin in the solution. The potato was chopped so that the blender did not need to work as hard to break open the cells. The instructor then placed the chopped, peeled potato into a chilled blender. The blender is chilled as heat will speed up the rate of reaction. Cold (chilled) distilled water was then added to the potatoes. This was done to break open the cells of the potato. The catecholase and cofactors are inside the potato cells; water is…Many heavy metals are used in antiseptics. Explain the oligodynamic effect and provide a clinical example of the use of heavy metals.