. Use the table of completely made-up data below to answer the following questions about a completely made-up enzyme. Enzyme no enzyme wild type R225L R58L E167A K(AM) 5.8 x 10* 4.9 x 10 3.3 х 10 4.1...

6. Use the table of completely made-up data below to answer the following questions about a completely<br>made-up enzyme.<br>Enzyme<br>no enzyme<br>wild type<br>R225L<br>R58L<br>E167A<br>K(AM)<br>5.8 x 10*<br>4.9 x 10<br>3.3 х 10<br>4.1 x 10<br>2.8 x 10<br>8.1 x 102<br>6.7 x 10<br>2.2 x 10<br>100.8<br>8569<br>88:4<br>11724<br>E201A<br>105.6<br>196л<br>98.8<br>C14A<br>TI1.7<br>a. Using the information in the table above, approximately what is the fold rate enhancement<br>for the wild type enzyme compared to the non-enzymatic reaction? '<br>b. Six different active site amino acid mutant enzymes were studied here. Comparing these<br>to the wild type, which of the amino acids listed play a role in catalysis?

Extracted text: . Use the table of completely made-up data below to answer the following questions about a completely made-up enzyme. Enzyme no enzyme wild type R225L R58L E167A K(AM) 5.8 x 10* 4.9 x 10 3.3 х 10 4.1 x 10 2.8 x 10 8.1 x 102 6.7 x 10 2.2 x 10 100.8 8569 88:4 11724 E201A 105.6 196л 98.8 C14A TI1.7 a. Using the information in the table above, approximately what is the fold rate enhancement for the wild type enzyme compared to the non-enzymatic reaction? ' b. Six different active site amino acid mutant enzymes were studied here. Comparing these to the wild type, which of the amino acids listed play a role in catalysis? " c. Which of the amino acids listed are important for binding to the substrate, but not necessarily for catalysis? ("

Jun 11, 2022
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