A biochemist is trying to determine the type of proteases they have isolated from walrus blubber.The three proteases and their relative activities in the presence of the indicated non-specificirreversible inhibitors are shown in the table below:Protease aProtease BProtease yGiven this data, please answer the following question:The catalytic site of Protease ß contains an important:CRH+ lodoacetateNormal ActivityNormal ActivityNo ActivityU+ TetranitromethaneNormal ActivityNo ActivityNormal Activity For the following calculations, please provide your answers in whole numbers (nodecimals).A research group has discovered a new enzyme they denote XC-95, which catalyzes theconversion of its substrate, propanol, to propionic acid, the product. The researchers begin tocharacterize the enzyme.In the first experiment, with [E]=4x10-5 mM, they find that Vmax=4 μM s-1. Based on thisexperiment, the kcat for XC-95 in units of s-1 is. In their second experiment, with[propanol]=0.01 mM, the researchers find that vo-2000 nM s-1. The measured KM of XC-95 forpropanol in units of µM isA/ Further researchshowed that the purified XC-95 used in the first two experiments was actually contaminated with areversible inhibitor of the enzyme, butanol. When butanol is removed from the purified enzyme andthe first two experiments are repeated, Vmax is found to be 4 µM s-1, and the measured KMbecomes 10 μM. Based on this new data, the mechanism of inhibition by butanol is BESTdescribed by which of the following:CompetitiveUncompetitiveMixedNon-competitiveand the value of a is

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Answered: A biochemist is trying to determine the…

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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Two isoforms of an enzyme were discovered; isoform-1 produces a hormone that causes muscle spasms and isoform-2 makes a different hormone (from the same substrate) that lowers cholesterol levels. a) What strategy would you employ as a medicinal chemist to develop a drug that prevents muscle spasms without raising cholesterol levels? The active sites of isoform-1 and -2 are the same except isoform-1 has a cysteine residue and isoform-2 has a phenylalanine residue at that same position. b) What two approaches would you take for designing a muscle spasm drug without a cholesterol level increase side effect?
Describe a common feature at the active site of serine proteases and acetyl cholinesterase
Compounds I, II, and III are in the following biochemical pathway: precursor compound I enzyme A enzyme B compound II ► compound III enzyme Mutation a inactivates enzyme A, mutation b inactivates enzyme B, and mutation c inactivates enzyme C. Mutants, each having one of these defects, were tested on minimal medium to which compound I, II, or III was added. Fill in the results expected of these tests by placing a plus sign (+) for growth or a minus sign (-) for no growth in the table below. Minimal medium to which is added Strain with mutation Compound I Compound II Compound III
The following data describe the catalysis of cleavage of peptide bonds in small peptides by a protease: Substrate K (1/s) K₁, (mM) k./K₁ (mM/s) A 0.1 10 B 1 1 10 0.1 100 0.02 8,000 0.05 10,000 0.5 Use this information to answer the next three questions. BODEF с D E F 0.01 1 100 5,000 160,000 20,000 4. Which substrate binds to the enzyme with the highest affinity? a. A b. B C. C d. D e. E f. F
When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
Please provide Typed solution in details, you can use only handwritten diagram
Parts of the mechanism for lysozyme are shown below. The catalytic lysozyme residue side chains can be identified as being above and below the polysaccharide chain shown at point A. Complete the missing structures (points B and E) and curly arrows (points A, B, C, D and E) in the mechanism, as well as from the knowledge you have gained, label the catalytic amino acids at point A in your mechanism with their correct name and residue number. A OH R OH O-R H₂C- HO NHAC NHAC E R D OH B R C H RO H3C- ° H₂C- NHAC Y R OH NHAC R R
Acid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters as follows; R-O-P-O3-2+ H 20 OR-OH + HO-P-O3-2. Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostate gland. The enzyme from the prostate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostate gland. Tartrate ion can strongly inhibit the phosphatase from the prostate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum?
I have an aqueous solution of tyrosinase but I require the solid form of tyrosinase. How would you process the aqueous solution to obtain the solid form?
the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu
The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?
Which strategies listed does this enzyme use to facilitate cleavage of α-galactoside? Choice 1 of 6:Dehydration synthesis Choice 2 of 6:acid base catalysis Choice 3 of 6:covalent catalysis Choice 4 of 6:metal ion catalysis Choice 5 of 6:stabilizing the transition state Choice 6 of 6:binding with high affinity to the product

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