The comparison of chymotrypsin and subtilisin active site geometries on the assumption that their similarities had catalytic importance has improved mechanistic knowledge of both enzymes (which they did not). Is this technique effective?

The comparison of chymotrypsin and subtilisin active site geometries on the assumption that their similarities had catalytic importance has improved mechanistic knowledge of both enzymes (which they did not). Is this technique effective?

Basic Clinical Laboratory Techniques 6E

6th Edition

ISBN:9781133893943

Author:ESTRIDGE

Publisher:ESTRIDGE

Chapter6: Basic Clinical Chemistry

Section6.5: Blood Glucose And Hemoglobin A1c

Problem 8RQ

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The comparison of the active site geometries of chymotrypsin and subtilisin under the assumption that their similarities have catalytic signifi cance has led to greater mechanistic understanding of both these enzymes. Discuss the validity of this strategy.
Increased mechanistic knowledge of both chymotrypsin and subtilisin enzymes has emerged from comparing their active site geometries in the hope that their commonalities would have catalytic importance (which they did not). Are you able to discuss the efficacy of this strategy?
Comparing chymotrypsin and subtilisin active site geometries on the assumption that their similarities have catalytic importance has improved mechanistic knowledge of both enzymes (which they did not). Can you evaluate this approach?
Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?
Mechanistic insights into the catalytic mechanisms of chymotrypsin and subtilisin were gained by a comparison of their active site geometries (which they did not). What do you think of the effectiveness of this strategy?
What method and conditions (provide detail) do you propose to measure the Specific Activity of the enzyme chymotrypsin?
(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90
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The Commercial Trainee Program of the Pharma Biotec Industry, opened selection to admit candidates who would help in the development of a more efficient production protocol of Ibuprofen, a non-colloidal anti-inflammatory. Basically, the challenge stimulated obtaining high enantiomeric purity of the final product. In this way, the candidates proposed the use of immobilized enzymes for the process. Tick the most coherent alternative to justify the choice of using immobilized enzymes by the candidates for the case mentioned above in the question. (Only one statement is true)* A)The use of immobilized enzymes was an interesting strategy, since different immobilization techniques can be used, such as adsorption and covalent. b) The use of immobilized enzymes was consistent since the immobilization process can further favor the regioselectivity , enantioselectivity and stereoselectivity properties of the enzymes, which will favor the enantiomeric purity of the drug. c) The use of…
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