4. I would like you to design a process for producing the amino acid threonine (C4H9O3N;MW-119.1) using E. coli cells (CH1.800.5 No.2). Your carbon and nitrogen sources will beglycerol (C3H8O3, MW =92) and ammonia (NH3), respectively. Small-scale experimentsshowed that we can achieve the following cell and product yields: Yxs = 0.2 g cell/g glycerol,YP/S 0.15 g threonine/g glycerol.a. (15 pts) Assuming that cell growth and threonine production occurred simultaneously,write a balanced stoichiometric reaction for this biological process.(92% of the E. coli dry cell weight is composed of C, H, O, and N. Their atomic massesare 12, 1, 16 and 14, respectively.)b. (4 pts) What is the product yield on cells (YPX; g threonine/g cell)?c. (3 pts) Two other mutated strains of E. coli have YP/S = 0.28 g threonine/g glycerol and YP/S= 0.05 g threonine/g glycerol, respectively. When you compare these mutated strains,d you replace it with any

Answered: 4. I would like you to design a process…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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5) The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences. al.H.colbe91srtihot wolsd sldu non lom i anolterineon mundillups betsmus 8880
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…
Draw the product that is immediately formed when this compound reacts under the conditions described here in your template in the box labeled Problem C2. Indicate clearly whether this compound is radiolabeled by indicating the position of the labeled atom. Cells that were actively undergoing fat catabolism were isolated and bathed in a medium containing radiolabeled (13C) bicarbonate (HCO3"). Answer the questions about this specific fat remnant under these conditions. SCOA
4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
Can someone please help me with these two questions, please hurry I only have 45 minutes;
Cysteine proteases are enzymes that degrade proteins. You may have heard of some examples of these types of proteins before! Bromelain is an enzyme found in pineapple that is commonly used as a meat tenderizer and is the reason Jell-O with fresh pineapple will not solidify. Cysteine proteases are remarkably similar to serine proteases (like chymotrypsin), except they have a cysteine in their active site rather than a serine. Using the mechanism that we discussed for serine proteases, draw a corresponding mechanism for a cysteine protease cleaving the bond between an alanine-glycine dipeptide. Note that cysteine proteases do not require an aspartate in their active site. Also note that the cysteine is usually in its thiolate form (deprotonated) and the histidine is in its imidazolium form (fully protonated) in the resting state of the enzyme.
Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.
What is the mechanism of an enzyme reaction involving a coenzyme for Nucleophilic Addition Rxns? Give
The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. ()
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).
A rat liver (2 gms) was dissected, homogenized under optimal conditions in appropriate buffer (50 ml), pH, temperature & supplemented with protease inhibitors. The protein level in a 100 μl sample of the homogenate (H) was determined using standard procedures, & was estimated to be 2 mg/ml. Peepo is a medical student interested in purifying a protein that transports copper (Cu) at the expense of ATP hydrolysis into ADP and inorganic phosphate (Pi). Thus, prior to purification Peepo must develop an assay/test that confirms the presence of this protein. Kindly select one answer for Questions 1-10 Question -1 Compared to a control which of the following may serve as a possible assay verifying the presence of a Cu sensitive protein that hydrolyzes ATP: Add Cu to the H and measure the level of Pi Add ATP to H and measure the level of copper Vary copper level, add inorganic phosphate to H & measure residual Pi Vary Cu, add ATP to H and measure level of inorganic Pi…
Can somebody help me with this question? I dont understand it. Thank you.

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