. The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in itsnonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pKvalues for the side-chain carboxyl groups on the two amino acids in solution are virtuallyidentical.a) How can one carboxyl group be charged and the other uncharged in the active site oflysozyme?b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreasesabove and below this optimum?Glu3sNAGAsp520-HGlu35 -CAsp52tri-NAGNAG

The lysozyme is an enzyme found in the secretions like tears and sweat. It cleaves the glycosidic…

Answered: The mechanism for lysozyme cleavage 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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What role do low-barrier hydrogen bonds play in serine protease catalysis?
Suppose you discover that bacteria that express OmpF have concentrations of <0.1uM of ciprofloxacin in the cytosol but those without this substance have concentrations of up to 50uM in the cytosol by the time they die. What does this tell you about the function of the isolated substance, OmpF, which you suspected from the start was related to quinolone resistance? How is the OmpF structure optimized for this function? Which amino acids in OmpF are suited to each aspect of its function? The structure of ciprofloxacin is shown below for reference.
Which of the following statements comparing the synthesis of pyrimidines vs. purines is correct? (A) Both types of nucleotides are formed by constructing the nitrogenous base step-by-step on a phosphorylated ribose foundation.(B) Aspartate serves as a nitrogen donor only for purines, while pyrimidines use only glutamine as a nitrogen donor. (C) Both pathways require the synthesis of 5-phophoribosyl-1-pyrophosphate.(D) During the de novo synthesis of both types of nucleotides, nucleosides are formed first and then phosphates are added to the 5’ carbon of ribose.(E) Ribonucleotide reductase is used to form dNTPs from pyrimidine NTPs but not purines.
What would the order of migration be (bottom to top in the gel) in a SDS-PAGE for the following proteins? Concanavalin A (ConA) (a homotetramer of 106 kDa), lysozyme (a monomer of 14.3 kDa) & horse liver alcohol dehydrogenase (ADH) (a homodimer of 80 kDa). a. ADH, ConA, lysozyme b. ConA, ADH, lysozyme c. Lysozyme, ADH, ConA Od. Lysozyme, ConA, ADH
1. A) Explain this statement, “Most enzymes are gene-encoded proteins, but most enzymes are not only protein". B) You recently isolated a new enzyme in your lab, and you named it "lipidase 1120". As a temporary name, this is fine. Who is responsible for assigning a formal name, and on what criteria will that name be assigned?
The purified OXA-M290 enzyme can now be tested to determine which β-lactamase inhibitor is most effective. This inhibitor could be prescribed in combination with a β-lactam antibiotic to treat the infection caused by the E. coli KGH1 strain. Before testing inhibitors against OXA-M290, the kinetic activity of this enzyme must first be measured. The activity of OXA-M290 is measured using nitrocefin, a chromogenic β-lactam antibiotic. When nitrocefin is hydrolyzed by a β-lactamase, it changes from yellow to red in colour. The nitrocefin hydrolysis product has an extinction coefficient of 20,500 M-1 cm-1 at 486 nm. The hydrolysis of 60 μM nitrocefin by 1 nM OXA-M290 is monitored using a microplate reader. The absorbance of the wells in the plate is measured at 486 nm every 30 seconds. This experiment is carried out with three replicates, generating the following data: Time (min) Absorbance of Replicate 1 Absorbance of Replicate 2 Absorbance of Replicate 3 0.5 0.0984…
Why is de novo biosynthesis of purines markedly elevated in patients with a deficiency in hypoxanthine-guanine phosphoribosyl transferase (HGPRT)? 5-Fluoruracil is converted to methotrexate by a DPD deficiency, leading to increased purine biosynthesis. HGPRT deficiency prevents purine salvage, leading to increased purine biosynthesis to make up for it. HGPRT increases pyrimidine salvage and thereby increases purine biosynthesis as a result. Increased purine biosynthesis is the result of ATP hydrolysis during the production of cyclic AMP.
We learned that three different amino acid transformations of PLP-dependent enzymes canresult from different conformations of the PLP-amino acid imine adduct in the active site.Starting from the PLP adduct of (S)-serine, show mechanisms fora) Decarboxylation of serineb) Racemization of serinec) Conversion of serine to glycine and formaldehyde.
Since all of the B-lactams that you have tested are susceptible to hydrolysis by PAESBL-1, the hospital will not be able to use a single 8-lactam to combat this P. aeruginosa isolate. You need to consider alternative strategies. From the following list, select all of the strategies that might successfully overcome the broad substrate specificity PAESBL-1: Check all that apply. using multiple B-lactams simultaneously (e.g., rather than treating with amoxicillin alone, treat with the three B-lactams: amoxicillin, cephalothin, and imipenem). O using a reversible inhibitor of PAESBL-1 instead of a 8-lactam. Treat future infections by O combining a reversible inhibitor of PAESBL-1 with one or more 8-lactams. O using an irreversible inhibitor of PaESBL-1 instead of a B-lactam. O combining an irreversible inhibitor of PAESBL-1 with one or more -lactams. O O O O
Within the body, CoQ 10 can be found in an oxidized or reduced form (also known as ubiquinone and ubiquinol). Describe how these structures differ and the biochemical role of coenzyme Q10.
The biosynthetic pathway for the two amino acides E and H is shown schematically in the Figure below: A W E 2 Z H How would this pathway change if C was mutated and non-functional?
The majority of bacterial mutations that need isoleucine also require valine for growth. Why? Which enzyme or process would be deficient in a mutant that requires solely isoleucine for growth (rather than valine)?

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