8L.3.4 Construct a graph of the rate of reaction as a function of PNPA concentration for the trypsin-catalyzed hydrolysis.Histidine rate(mm/min)Trypsin rate(mm/min )0.00430.0200.00680.0410.01720.1020.03420.1850.06910.2650.1650.3560.3520.4920.5150.5200.6840.525Plot rate versus concentration using the graph label Trypsin: catalyzed hydrolysis from 0 to 20 mM.+*No elements selected[pNPA](mm)0.10.20.51.02.05.010.015.020.0trypsin rate (mm/min)0.500.400.300.200.105.010.015.020.0?

we have to plot graph between trypsin rate and pNPA.

Answered: Construct a graph of the rate of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Gout is characterized by elevated uric acid concentrations in blood and urine due to a variety of metabolic abnormalities that lead to the overproduction of purine nucleotides. Allopurinol is used in the treatment of gout because this drug, and its metabolic product, alloxanthine, act as inhibitors of: а) Xanthine Oxidase PRPP synthetase c) Hypoxhantine guanine phosphoribosyl b) Adenyl succinate synthase d) transferase e) Nucleotides
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
Discuss the role of enzymes in metabolic regulation by describing the following five mechanisms.11.1Cascade systems11.2 Futile cycle11.3Cellular compartmentalization 11.4 Covalent modification11.5 Zymogens
In some organisms, isoleucine can be synthesized in a multi-step procedure (a series of enzymatic reactions), beginning with a molecule of threonine. Keeping that in mind explain the experimental results below. Amount of endproduct Activity of threonine (isoleucine) deaminase None Low Medium High Very high High Moderate Very low
Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)
Consider an enzyme that catalyzes the reaction S2 P, by the following simple reaction mechanism: k, E + S 2 E•S →E kcat + P Suppose the enzyme acquires a mutation that causes k1 to be 10-times smaller than for the wild-type (non-mutant) enzyme. Suppose you measure the initial reaction rate (vo) at several different [S] for the mutant and the wild-type enzymes. Under what conditions would the mutation have a greater effect on the reaction rate (vo) of the mutant enzyme compared to the wild-type enzyme - at very low [S], or at very high [S]? Explain briefly how you decided.
Discuss the role of enzymes in metabolic regulation by describing the following mechanisms.11.1Cellular compartmentalization 11.2 Covalent modification11.3 Zymogens
There is an enzyme that catalyzes the production of the pigment responsible for dark fur color in Siamese cats and Himalayan rabbits. This enzyme is thermolabile, meaning that it does not function at higher temperatures. Rabbits raised at 5°C are all black. If raised at 20°C, they are white with black paws, ears, and noses; they are all white when raised at 35°C. Draw an activity curve for this enzyme, and explain.
One of your colleagues has obtained a sample of muscle phosphorylase b that is known to be relatively inactive. She has approached you for advice on how to set up an appropriate assay. She has the following items available, not all of which are appropriate for this study. Help her out by selecting the items that she should use and what their purpose is in the assay, and then explain why each of the other items would not be useful. 1. 100 UM AMP 2. 100 UM GTP 3.100 uM glucose 4. 100 uM glucose 6-phosphate 5. Branched glycogen 6. Amylose (i.e. unbranched glycogen) 7.50 mM HEPES buffer, pH 7.5 8. 50 mM potassium phosphate buffer, pH 7.5 Write out a short explanation for each of the above items, and upload your answers by the due date.
Consider the following data for an enzyme-catalyzedhydrolysis reaction in the presence and absence ofinhibitor I: Using a Michaelis-Menten plot, determine Km for theuninhibited reaction and the inhibited reaction.
Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of inhibitor you identified it as. If you were to add 5nM of a reversible inhibitor, the Km for the measured enzyme catalyzed reaction would ______ (Increase, Decrease, Stay the same) to ______µM (choose appropriate value) and Vmax would _______ (Increase, Decrease, Stay the same) to ______µMs-1. So, this inhibitor is a ______ (Competitive, Uncompetitive, Mixed) inhibitor. Conditions: kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
Consider a series of experiments in which 32P-labeled inorganic phosphate were introduced to erythrocytes (red blood cells) undergoing glycolysis. Would you expect to see the labeled phosphate in any glycolytic intermediates? If so, which and at what relative concentrations?

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