Chemical Digestion and its pH Levels Needed for Enzyme Breakdown (Lab 4)

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answer item no. 7-10

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9:34 AM You sent       Help me with this one Select true if the statement is CORRECT and false if OTHERWISE   1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…

BSC1010C Enzymes & Cellular Regulation Dr. Harris Amylase is an enzyme found primarily in saliva and pancreatic secretions. It catalyzes the breakdown of starch into sugars. A Rate of reaction 0 20 60 40 Temperature, C C Rate of reaction 80 100 B Rate of reaction Enzyme concentration (Substrate concentration always in excess) Substrate concentration (Enzyme concentration constant) The above graphs (A, B & C) provide data on several factors that affect the activity and function of amylase in living organisms. 11. What variables are compared in graph A? What information can be obtained from this data?

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What is the substrate of salivary amylase in both experiments?

urses / MEDBAS145en 21-22Spring / 2021-2022 Spring Semester / Final Which of the following pairs depict the absolute specificity of the enzyme? Select one: O O O O a. All of them b. Hexokinase - Glucose c. Lactase - Lactose d. Lipase - Triacylglycerol

Enzyme Investigation An enzyme was isolated from digestive juices taken from the small intestine. An experiment was set up to test the ability of the enzyme to break down protein. Two test tubes, labeled A and B, were placed in a hot water bath at 37°C, human body temperature. Test tube A contained only protein and test tube B contained protein and the enzyme. The chart below shows the set-up. After two hours, the contents of both test tubes were analyzed. Test tube A showed only the presence of protein. Test tube B showed the presence of the end products of protein digestion, indicating the enzyme had successfully broken down the protein. Identify the end products of protein digestion that made up the contents of test tube B after the two hours.

Please help with part a and b both the questions urgently within an hour

nment Score: 85.7% O Resources Lx Give Up? O Hint Check Answer on 13 of 23 > Attempt 4 The following tetrapeptide was digested completely with proteolytic enzymes. Modify the structure to show the amino acid hydrolysis products of this digestion, including the appropriate protonation and charge for each carboxyl and amino group at pH 7. Use the Erase tool to remove bonds where necessary. Select Draw Rings More Erase H H,N. CH, CH, CH, CH, OH acer

Topic: Processes of protein metabolism  Arrange the following statements regarding the processes of protein metabolism starting from Step 1 to Step 10.

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Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG

Course : BiochemistryChapter : Amino acid metabolism In the catabolic reaction of amino acids, ammonia is produced as a side compound.Ammonia is so poisonous that it must be removed from the body in the form of urea.Please explaina. the reaction of amino acids with ketoglutarate to produce ammoniab. the urea cyclec. where do reactions a and b occur? Please write the answer on paper ( Handwriting )And provide pict with detail explanation because i want to learn every steps of the processThank you

POST-ASSESSMENT Let's see how much you have learned. 1. Give five examples of Cofactors and Coenzymes and describe each. 2. Discuss the behavior of enzymes as described by the Michaelis-Menten Equation. 3. Differentiate Enzyme Inhibition by filling the table below: Competitive Non-Com petitive Uncompetitive Inhibition mechanism Km Vm 105 Copyright 2019. All Rights Reserved.

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Please complete Boothe parts of part B thoroughly with detailed explanations since only part A was done already. Thank you

Enzymatic Hydrolysis of Cooking Oil.

Select true if the statement is CORRECT and false if OTHERWISE   1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical reaction catalyzed. 9. The living cell is the site of tremendous…

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Need help with number 3

Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

Can you also answer al these questions please !! Thank you so much I really appreciate it a lot ?

Answer b and c

Topic: Co-Enzyme Q10   Question: What does it mean when asked to explain the evidence behind medicinal chemistry of the CAM agent, and if the chemical structures relate to it's effects.

please very soon full explanation all parts please 1a. Add to this drawing the substrate molecule binding to the active site and be specific about the shape of the substrate molecule. Next to your drawing write the chemical properties of the substrate that are important for it to bind to the enzyme. 1b. If the amino acid serine present in the active site were to be mutated to valine, how will this mutation affect the enzyme’s activity? Explain in 30 words or less. 1c.  Your colleague would like to design an inhibitor molecule for the normal version of this enzyme that targets the enzyme active site. What are two characteristics of the inhibitor that you would suggest they incorporate in order to allow it to maximally block the enzyme’s activity? Use 40 words or less.

Does anyone know the answers for any of these?