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- Staphylococcal nuclease has a ΔΔG‡ of -84.1 kJ mol-1 at 25.0 °C. If the uncatalyzed rate is 0.630x10-13 µmol s-1, calculate the enzyme-catalyzed rate in µmol s-1. (Use R = 8.3145 J mol-1 K-1)The substrate which was used to investigate the enzymatic activity of wheat bran phosphatase was p-nitrophenyl phosphate. It is converted to p-nitrophenol and inorganic phosphate by this enzyme. P-nitrophenol has a pKa of 7.1 and is colorless, while its conjugate base, p-nitrophenolate has a yellow color. The enzyme assay was performed at pH 5.1 after the 0.5 N KOH is added at the end of each enzyme assay, the pH of the assay mixture is raised to 9.1. Why was the base added?A number of auxotrophic mutant strains were isolated from wild-type haploid Neurospora crassa. These strains responded to the addition of certain nutritional supplements to minimal culture medium either by growth (+) or no growth (0) The data from this experiment are presented in the table below. Diagram a biochemical pathway, complete with positions of intermediates, that is consistent with the data. Indicate where in the pathway each mutant strain is blocked.
- Ibuprofen and indomethacin are clinically important inhibitors of prostaglandin H₂ synthase-1. Cells expressing this enzyme were incubated under four different conditions, after which the activity of the enzyme was measured by adding radiolabeled arachidonic acid and detecting newly-produced prostaglandin H₂: 1. 40 min without inhibitor (control) 2. 40 min with inhibitor 3. 40 min with inhibitor, after which the cells were resuspended in medium without inhibitor 4. 40 min with inhibitor, after which the cells were resuspended in medium without inhibitor and incubated for an additional 30 min The bar graphs show the results of the experiments with ibuprofen and indomethacin. The bars in each graph correspond to the four different incubation conditions. Ibuprofen Prostaglandin H₂ synthesized (relative to control) 100 80 60 40 20 I I I (1) (2) ll (3) (4) Prostaglandin H₂ synthesized (relative to control) 100k 80 60 40 20 I (1) Indomethacin (2) (3) (4)The activity of the enzyme β-galactosidase produced bywild-type cells grown in media supplemented with different carbon sources is measured. In relative units, thefollowing levels of activity are found:Glucose Lactose Lactose + glucose0 100 1Predict the relative levels of β-galactosidase activity incells grown under similar conditions when the cells arelacI−, lacIS, lacO+, and crp−.Pyridoxal phosphate (PLP) is a coenzyme for the enzyme ornithine aminotransferase. The enzyme was purified from cells grow in PLP = deficient media as well as from cells grown in media that contained pyridoxal phosphate. The stability of the two different enzyme preparations was then measured by incubating the enzyme at 37°C for different lengths of time and then assaying for the amount of enzyme activity remaining. The following results were obtained. (a) Why does the amount of active enzyme decrease with the time of incubation? (b) Why does the amount of enzyme from the PLP deficient cells decline more rapidly?
- The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-Dglucose 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 byglucose 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. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for measuring blood glucose?*The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of 3-D-glucose to D-glucono-6- lactose. This enzyme is highly specific for the ß anomer of In spite of this glucose and does not affect the a anomer. 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 3- and a-D- glucose. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quan- tities of glucose, what advantage does glucose oxidase offer over non-enzymatic oxidizing agents like Tollens reagent? *Is B-D-glucosamine a reducing sugar?Identify the effect of lowering the KM of phosphoglucoseisomerase on Phosphofructokinase activity. Group of answer choices Increased Activity Decreased Activity Activity Levels are not Changed
- J. C. Servaites, in Plant Physiol. (1985) 78:839–843, observed that Rubisco from tobacco leaves collected before dawn had a much lower specific activity than the enzyme collected at noon. This difference persisted despite extensive dialysis, gel filtration, or heat treatment. However, precipitation of the predawn enzyme by 50% (NH4)2SO4 restored the specific activity to the level of the noon-collected enzyme. Suggest an explanation.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…A marine microorganism contains an enzyme that hydrolyzes glucose-6-sulfate. The activity test is based on the measurement of the rate of glucose formation. The enzyme in a cell-free extract has a KM of 6.7 x 10-9 M and a Vmax of 300 nM min-1 . Galactose-6-sulfate is a competitive inhibitor of the enzyme. To a concentration of glucose-6-sulfate 2 x 10-5 M and galactose-6-sulfate 10-5 M, the speed initial is 1.5 nM min-1 . Calculate the Ki for galactose-6-sulfate.