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 objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…
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
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Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-A
Please provide Typed solution in details, you can use only handwritten diagram

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