For the attachment of a substrate to the active site of an enzyme: k1 S+E→ SE k-1 The equilibrium constant is measured 200. The forward reaction is 2nd order and the reverse is 1st. In a separate experiment, the rate constant for the second-order attachment was found to be kj = 1.5 x 108 dm3 mol-1 s-1. k.1 = ? choose one. 3.0 x 1010 dm3 mol-1 s-1 3.0 x 1010 7.5 x 105 7.5 x 105 s- 1

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For the attachment of a substrate to the active site of an enzyme:
k1
S+E→ SE
k-1
The equilibrium constant is measured 200. The forward reaction is 2nd order and the reverse is 1st.
In a separate experiment, the rate constant for the second-order attachment was found to be kj = 1.5 x 108 dm3 mol-1 s-1.
k.1 =
? choose one.
3.0 x 1010 dm3 mol-1 s-1
3.0 x 1010
7.5 x 105
7.5 x 105 s- 1
Transcribed Image Text:For the attachment of a substrate to the active site of an enzyme: k1 S+E→ SE k-1 The equilibrium constant is measured 200. The forward reaction is 2nd order and the reverse is 1st. In a separate experiment, the rate constant for the second-order attachment was found to be kj = 1.5 x 108 dm3 mol-1 s-1. k.1 = ? choose one. 3.0 x 1010 dm3 mol-1 s-1 3.0 x 1010 7.5 x 105 7.5 x 105 s- 1
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