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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A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.
Unbranched homopolymer of N-acetyl glucosamine is : 1.Cellulose 2.Chitin 3.Curcumin 4.Concanavalin A
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase A-ase Acetate Deacetylase D Protease B-ase C-ase A-ase ABC- What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition
In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectively
Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.
Describe a common feature at the active site of serine proteases and acetyl cholinesterase
Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1
complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
In biochemistry laboratories, phenylmethylsulfonyl fluoride (PMSF) is a serine protease inhibitor commonly added to cell homogenates to protect proteins from digestion form serine proteases that are released when cell membranes and cell organelles are broken. =S-F PMSF: phenylmethylsulfonyl fluoride 1. Based on our discussion of covalent inhibition of acetylcoline, esterase by diisopropylfluorophosphate, predict the effect of PMSF on chymotrypsin and predict how PMSF will modify the chymotrypsin active site. Justify your answer based on the propertied of the active sites of the enzymes.
To answer this question, please reference the Problem Solving Video: pH and pK, of an Amino Acid. Proteases are enzymes that cleave peptide bonds using general acid-base catalysis. General acid-base catalysis relies on a protor donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin's active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding. Asp 102 [His] [His+] His 57 6.0 -H-N Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to the presence of gastric juice, chymotrypsin often functions in an environment of pH 5.5-7.0. Incorrect The imidazole group of free histidine has a pK₂ of 6.0. Use the…

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