A research group discovers a new version of happyase, which they call happierase

Question

A research group discovers a new version of happyase, which they call happierase, that catalyzes the biochemical reaction The researchers begin to characterize the enzyme. In the first experiment, with [E] at 5 nM they find that the Vma IS 1.6 muM S^-1 Based on this experiment, what is the Kcat for happierase? (Include appropriate units). In another experiment, with [E] at 1 nM and [HAPPY] at 50 muM, the researchers find that Vo = 400 nM s1. What is the measured Km of happierase for its substrate HAPPY? (Include approprate units). Why are uncompetitive and mixed inhibitors generally considered to be more effective in vivo than competitive inhibitors? 100%

Explanation / Answer

Kcat= Vmax/E

Vmax= Maximum rate 1.6uM/s = 1.6*10-6M/s

and E= 5nM=5*10-9M

Kcat= 1.6*10-6/ 5*10-9 =320sec-1

b) V= Vmax[S]/ [KM+S] S= Substrate concentration = 50*10-9 M

400*10-9= (1.6*10-3*50*10-9 )/ ( KM+ 50*10-9)

KM+ 50*10-9= 1.6*10-3*50*10-9/ 400*10-9=1.6*10-3*50/400= 1.6*10-3*0.125 =2*10-4

Km= 2*10-4-50*10-9 =0.0001995M

6. In case of competitive inhibition, the substrate and inhibitor competes for occupying the active site of the enzyme

in case of uncompetitive and mixed inhibitors, the enzyme binds to the Enzyme substrate complex.

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