You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme'sinactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin.The difference in specificity might be explained by theabsence of the S1 binding pocket.replacement of serine 195 with a positively charged residue.presence of a positively charged residue in the S1 binding pocket.presence of a negatively charged residue in the S1 binding pocket.

In the realm of enzymology, understanding the specificity of proteases is crucial for unraveling…

Answered: You have isolated a new protease that…

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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Similar questions

The enzymes GICNAC phosphotrasnferase is a key enzyme involved in the transporting of proteins from the trans-Golgi to the lysozyme. In addition to the catalytic function of the enzyme that involves certain sugars, what is the second critical function of this enzyme? O It recognizes internal signal sequences found on lysozyme-targeted proteins. O It drives the binding of a phosphorylated GlcNac group onto a mannose residue. O It facilitates the reversible binding of specific proteins to the M6P receptor O In is essential for the recruitment of clathrin triskelions to the budding vesicle.
An enzyme that follows the MWC (concerted) model for allostery has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation were to reverse that ratio (T/R = 1/300 = 3.3 x 10–3 in the absence of any substrate). How would this mutation affect the relation between the rate of the reaction and substrate concentration, i.e., what would a Vo vs. [S] plot look like, and why?
GTP-y-s serves as an analog of GTP that cannot be hydrolyzed any further. How would a Co-IP experiment differ between G- alpha & G-beta proteins in the presence of GTP-y-a and GDP?
Neuraminidase (NA) catalyzes a hydrolysis of the glycosidic linkages of sialic acids using a mechanism shown in Fig. (a). and Fig. (b) shows competitive inhibitors of NA Considering the mechanism of NA, why do zanamivir and oseltamivir inhibit NA so potently?
The researchers working on happyase discover that the compound STRESS is a potent competitive inhibitor ofhappyase. Addition of 1 nM STRESS increases the measured Km for SAD by a factor of 2. What are the values for α and α′ under these conditions?
Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. The saccharide was cleaved from its sialic acid residues. The treatments and results are as follows: 1. hydrolysis by B(1-> 4) - disaccharide products 2. hydrolysis by a(1-> 4) - release of 2 disaccharide & 2 monosaccharide units. Show the structure of the saccharide.
Consider a hypothetical enzyme that is COMPLETELY deactivated when a Valine (Val) residue buried in the core of the enzyme is mutated to Glutamate (Glu). In one or two sentences max, explain the MOST LIKELY reason for this occurrence.
. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)
Some protein kinases are inactive unless they are phosphorylated on key serine or threonine residues. In some cases, active enzymes can be generated by mutating these serine or threonine residues to glutamate. Explain. What could you predict about a mutant generated replacing the serine or threonine with alanine.
Some strains of bacteria or microorganisms have developed toxins that can modify the activity of the alpha subunit of G proteins which results in disease. For ex. cholera toxin, produced by Vibrio cholerae, causes ADP ribosylation of the stimulatory Gαs subunit of G proteins. This modification abolishes the GTPase of Gαs, and results in an αs subunit that is always in the “on” or active state. It results in continuous stimulation of adenylyl cyclase (AC). The main cells affected by this are the epithelial cell in gastrointestinal tract. Knowing this altered activity of AC, explain why patients affected by this toxin experience severe diarrhea and dehydration that may result in death.
Based on your understanding of the structure and function of the enzyme chymotrypsin, explain why proteolytic activation by Trypsin in the intestine is required for chymotrypsin to bind its substrates with high affinity. Your answer should include a description of the amino acid residue or residues involved AND a kinetic experiment that suggested this.
Explain why a protein tyrosine phosphatase would include an SH2 domain in addition to its phosphatase domain.

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