Biochemistry

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answerhappygod
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Biochemistry

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Biochemistry
Biochemistry 1
Biochemistry 1 (78.86 KiB) Viewed 6 times
Biochemistry 2
Biochemistry 2 (78.86 KiB) Viewed 6 times
c) How many reactions does each enzyme active site catalyze per second when saturated with substrate in the absence of the inhibitor? (Show your calculations and be sure to include units.) K₂ = Vmax [[-] = (50 micro moll min) = 0.0625 x 10 2 T (800 pico mol) d) Is the maximum rate for the uninhibited reaction diffusion limited? Explain: e) Where on the enzyme molecule, relative to the active site, does the inhibitor most likely bind? Explain f) What is the value for the dissociation constant, Kj, of the inhibitor-enzyme complex?

c) How many reactions does each enzyme active site catalyze per second when saturated with substrate in the absence of the inhibitor? (Show your calculations and be sure to include units.) K₂ = Vmax [[-] = (50 micro moll min) = 0.0625 x 10 2 T (800 pico mol) d) Is the maximum rate for the uninhibited reaction diffusion limited? Explain: e) Where on the enzyme molecule, relative to the active site, does the inhibitor most likely bind? Explain f) What is the value for the dissociation constant, Kj, of the inhibitor-enzyme complex?
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