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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Similar questions

We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…
For production of penicillin (C16H18O4N2S) using Penicillium mold, glucose (C6H12O6) is used as a substrate and phenylacetic acid (C3H8O2) is added as a precursor. The stoichiometry for overall synthesis is: 1.67 C6H1206 + 2NH3 + 0.502+ H2SO4+ C3H8O2 → C16H180,N2S + 2CO2+ 9H2O a) What is the maximum theoretical yield of penicillin from glucose in g/g? b) When results from a particular penicillin fermentationvere analyzed, it was found that 24% of the glucose had been used for growth, 70% for cell maintenance activities (such as membrane transport and macromolecule turnover) and only 6% for penicillin synthesis. Calculate the yield of penicillin from glucose in g/g under these conditions. c) Batch fermentation under the conditions described in part b) is carried out in a 100-liter tank. Remember that only 6% of the glucose is used for penicillin synthesis. Initially, the tank is filled with nutrient medium containing 50 gL glucose and 4 g L phenylacetic acid. If the reaction is stopped…
For production of penicillin (C16H18O4N2S) using Penicillium mold, glucose (C6H12O6) is used as a substrate and phenylacetic acid (C3H3O2) is added as a precursor. The stoichiometry for overall synthesis is: 1.67 C6H1206 + 2NH3 + 0.502+ H2SO4+ C8H3O2 → C16H1804N2S + 2CO2+ 9H2O a) What is the maximum theoretical yield of penicillin from glucose in g/g? b) When results from a particular penicillin fermentation were analyzed, it was found that 24% of the glucose had been used for growth, 70% for cell maintenance activities (such as membrane transport and macromolecule turnover) and only 6% for penicillin synthesis. Calculate the yield of penicillin from glucose in g/g under these conditions. c) Batch fermentation under the conditions described in part b) is carried out in a 100-liter tank. Remember that only 6% of the glucose is used for penicillin synthesis. Initially, the tank is filled with nutrient medium containing 50 g L' glucose and 4 g L phenylacetic acid. If the reaction is…
Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3D
To determine whether this organism is capable of performing carbohydrate metabolism, ateam of researchers of which you are a part wanted to isolate an enzyme calledglyceraldehyde 3-phosphate dehydrogenase (GAPDH). The enzyme has the followingproperties. Number of amino acids: 335 Molecular Weight: 36,053 DapI: 8.57 Your project leader wanted you to present a basic purification protocol of GAPDH from theorganism based on the given properties above. Give a 1-sentence explanation for each stepof your protocol.
We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
Human blood serum contains a class of enzymes known as acid phosphatases, which hydrolyze biological phosphate esters under slightly acidic conditions (pH 5.0): R-O-P-O3-2 + H2O --> R-OH + HO-P-O3-2. Acid phosphatases are produced by erythrocytes, the liver, kidney, spleen, 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. The phosphatase from the prostate gland is strongly inhibited by tartrate ion, but acid phosphatases from other tissues are not. How can this information be used to develop a commercial specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum? * 1. Prostate cancer cannot be diagnosed biochemically. 2. Use tartrate to inhibit phosphatase from prostate gland and then subtract the results from the total serum enzyme activities to get an…
4.2 The first step in amino acid catabolism usually involve transamination. Since ammonia is a serious neurotoxin, the body maintains the nitrogen and ammonia balance carefully. Discuss the pathway, organelle and organs involved in maintaining this balance. Provide a schematic presentation of the pathway to supplement your discussion.
You are interested in purifying an enzyme X and decide to use an affinity chromatography followed by an enzymatic assay. You obtain the following data: Total volume of [protein] the sample (ml) (mg/mL) (U) |Total activity Sample name Specific activity |(U/mg) |Affinity | chromatography 2 0.12 5000 20833 You have obtained a 10X fold purification and a yield of 10% at the Affinity step. What was the protein concentration of your crude lysate sample, if its volume was 15 mL? Detail your answer by showing the calculations, and do not forget the UNITS!
Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
1. A Lineweaver-Burk Plot is shown below. 30 25 Curve A y = 3.1207x + 2.4978 20 15 Curve B y = 1.0003x + 2.3602 10 5 -3 1 5 7 11 1/[Catechol] (mM1) With these curves, determine the following enzyme parameters. Show all pertinent solutions. a. Km of Curve A and Curve B b. Vmax of Curve A and Curve B c. Assuming that one of these curves corresponds to the kinetics of one enzyme and one substrate, which curve represents the effect of an inhibitor? Why do you say so? d. What type of inhibition is exhibited by your answer in question c? Why do you say so? 1/V, (units of activity 1)
Table 4. Rates of saponification at 35°C. Ester k(M-' sec") k, relative* (CH,O),PO, 2.0 x 10 3.4 x 10-4 1.0 x 10-2 1.0 2 x 10 5 x 10 CH,CO,C,H, "Rate relative to that of (CH,O);PO;". Question 3 Table 4 lists the rates of base catalyzed hydrolysis (saponification) for several different esters. Using your understanding of nucleic acids chemistry, explain why hydrolysis of the phosphodiester is slow compared to the phosphotriester and ethyl ester.

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