Enzymes Lab Report_BIO1511_Win2023

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…

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…

200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.

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1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…

I2 An immobilized enzyme plug flow reactor (PFR) contains a very porous honeycomb structure that has an enzyme immobilized on its surface. The substrate (S) enters the reactor at a concentration of 0.05 mole L-1along with an uncompetitive inhibitor (I) with a concentration of 0.01 mole L-1. The enzyme properties are such that: Vmax= 1.2 x 10-8mole cm-2sec-1, Km= 0.12 mole L-1. For the inhibitor KI= 0.05 mole L-1. The flowrate through the reactor is such that kL= 10-4cm sec-1. The surface area to volume ratio of the honeycomb structure in the bioreactor is 1 cm-1. Estimate the residence time needed to achieve a 90 % conversion of the substrate. If the flowrate through the reactor is 100 L hr-1, what is the total volume (L) of the reactor needed to achieve this conversion? If the L/D ratio of the reactor is 10, what are the dimensions (ft) of the reactor? Repeat these calculations if external mass transfer effects are ignored.

A purified protease enzyme from the fungus Aspergillus sp. Is tested in a laboratory. This enzyme was lyophilized as a white powder. When reconstituting with phosphate buffer pH 7.2 the active enzyme is obtained. To check its purity, an electrophoresis is performed where a single band of approximately 70,000 molecular weight is observed. The solution with enzymatic activity was stored at 4ºC for later use. A few days later it was found that the enzymatic activity had been lost and in the electrophoretic analysis, instead of a single band there were three bands of weights 40,000, 20,000 and 10,000. Come up with a reasoned explanation of what might have happened to the enzyme

[One - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly

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The milieu wherein enzymes occur in vivo is dramatically different from in vitro experiments, which is often used to investigate enzyme. Give an overview of this as well as the nature of enzyme reactions in vivo. Name, in addition, the factors affecting the concentration of enzymes in vivo.

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Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3D

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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

I. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.

Enzyme Combination - Cla I + EcoRI  What is the number of fragments? What are/is the size(s) of fragment(s)?

Given the active site and reaction mechanism below, what is the mechanism of irreversible inhibition of the inhibitor provided? Active Site Reaction Mechanism Inhibitor `NH2. н Он SH OH- OH OH HO- NH „NH OH OH OH -Mg²+ Uncompetitive Affinity-based Transition state analog Non-specific Mechanism-based

ENZYME CATALYSIS LAB EFFECT OF TEMPERATURE   What chemical reaction is being catalyzed in this experiment? Label the substrate(s), enzyme and product(s).

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K = 5 μm V = 10 μm/s

Enzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.

AutoSave 301-Enzyme Kinetics and Inhibition, Part 2 - Compatibility Mode - Word Search ff steve M SM File Home Insert Draw Design Layout References Mailings Review View Help E Share O Comments Navi. Enzyme Kinetics and Inhibition, Part 2 Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor B for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor B (plus the control, with zero mM of inhibitor B). The following Table lists the inhibitor B concentrations [I], substrate concentrations [S], and resulting enzyme velocities (Vo) for all six of these experiments: 中 Search docume o v Headings Pages [S] [I] O mM 0 mM O mM O mM O mM 0.1 mM Vo 0.333333333333 mM per minute 1/[S] 1/ Vo Create an interactive 0.1 mM outline of your 0.2 mM 0.50 document. 0.3 mM 0.60 0.4 mM 0.666666666667 0.5 mM 0.714285714286 It's a great…

Please answer  a and b both

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Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case?     Word limit 180 words including citation and reference

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…

Factors Affecting Enzyme Activity: Catalase 3. What is the marker for the enzyme’s optimum condition?

Hello, I am comparing the four types of enzyme inhibition. Kidnly please fill out the table for me :)

The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below(white pitcure) suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance.