After solving the crystal structure of a novel enzyme and looking at the active site, a researcher makes the following point mutations to test which residues are involved in the catalysis, binding, or both. The total enzyme concentration is 4 uM in each test. Here are the results: Wild Type (unmutated enzyme) His64 Ala64 Arg12- Ala12 Asp121- Alat4 18015 3500 50 5501 10 8015 18117 3465 45 1000 20 35501 30 Calculate the catalytic efficiency for the wild type enzyme.

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After solving the crystal structure of a novel enzyme and looking at the active site, a researcher makes the following point mutations to test which
residues are involved in the catalysis, binding, or both. The total enzyme concentration is 4 uM in each test. Here are the results:
K luM)
Karfsec)
Wild Type (unmutated enzyme)
18015
3500 t 50
His64 Alab4
Arg12- Ala12
Asp121 Ala64
550 1 10
805
18117
3465 t 45
1000 20
3550 30
Calculate the catalytic efficiency for the wild type enzyme.
Transcribed Image Text:After solving the crystal structure of a novel enzyme and looking at the active site, a researcher makes the following point mutations to test which residues are involved in the catalysis, binding, or both. The total enzyme concentration is 4 uM in each test. Here are the results: K luM) Karfsec) Wild Type (unmutated enzyme) 18015 3500 t 50 His64 Alab4 Arg12- Ala12 Asp121 Ala64 550 1 10 805 18117 3465 t 45 1000 20 3550 30 Calculate the catalytic efficiency for the wild type enzyme.
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