2. (the active site in the Michaelis complex of a-chy-motrypsin and a polypeptide substrate. Describebriefly the catalytic or structural roles of the: To the right is a schematic diagram ofHis $7residues listed below:HOSer 195(а) Ser195AAn-C-ÇH-NH-ÇÇH-NH -AAnRHH.-N-195193GlySer(b) His57(c) NH groups of Gly193 and Ser195(d) The most favorable side chain R for binding(e) Identify the scissile bond with an arrow, i.e., the bond in the peptide substrate that is cleaved as aresult of the catalytic action of the enzyme. You can point to it on the diagram above.

Chymotrypsin is a protease that cleaves a peptide at the C-terminal of all aromatic amino acid.…

Answered: 2. ( To the right is a schematic…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 22P

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6 (a) A decapeptide has the following amino acid composition: Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. From the experimental data, deduce the primary structure of the decapeptide. (b) Suggest a scheme you will follow to synthesize the dipeptide Ala-Gly
3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however they are a structurally diverse family of enzymes especially in the organization of the active site amino acids. A group of scientists have reported a potential drug molecule based on a binding study using circular dichroism. They report that the molecule binds to the active site. Can the experiment support the claims, why or why not? Which techniques might be used to support this claim?
1. 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 2O  R-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 canyou 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?
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
8. The chemical structure of Coenzyme A contains the following except— a phosphoanhydride moiety. a β-mercaptoethylamine residue. a lipoic acid residue. a pantothenic acid residue. an adenosine-3’- phosphate.
Bovine chymotrypsinogen has a molecular massof 25.6 kDa. Amino acid analysis shows that thisenzyme is 4.7% Gly (Mr 75.1).b. Calculate how many glycine residues are present in amolecule of bovine chymotrypsinogen
If D-glyceraldehyde-3-phosphate (DGAP) is dissolved in water, 96% of it will form dihydroxy- acetonephosphate (DHAP). Which of the following will triose phosphate isomerase do? a)Shift the balance to 100% DHAP b)Shift the balance to 0% DHAP c)Shift the balance to 50 DGAP : 50 DHAP d)Catalyze the peptide bond breaking e)Make the reaction faster
4 How do I convert from DPM to picomoles per milligram of protein (pmol/mg)? I have the specific activity as [3H]-spiperone is 25530 DPM/pmol. is there an equation?
1. The Fehling’s reaction, which is a simple assay for reducing sugars, was used as a diagnostic test for the determination of blood glucose concentrations for a very long time. However, it has now been replaced by the glucose oxidase test. The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone. This enzyme is highly specific for the β-anomer of glucose and does not affect the α-anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose—that is, for solutions consisting of a mixture of β- and α-D-glucose. Explain how this is possible. Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for the determination of blood glucose? 2. Consider only the oxygen levels present in the cytoplasm and ECF as shown in the drawing above (no new oxygen is entering…
In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?
#1)What are the main roles of the following amino acids; (within the crystal structure and/or active site. be specific, with pictures and mechanistic arrows as needed) -Glu305 from pyruvate carboxylase -Gln23 from Penecilin Acylase -Ser203 from Acetylcholinesterase #2) Why is L-tetrahydro-2-furoic acid would be a suitable inhibitor for Proline oxidase?

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