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VARVARA [1.3K]
3 years ago
13

An inhibitor is added to an enzyme-catalyzed reaction at a concentration of 26.7 μM. The Vmax remains constant at 50.0 μM/s, but

the KM increases by 150%. Calculate the Ki for this inhibitor.
Chemistry
1 answer:
fomenos3 years ago
5 0

Using the Michaelis-Menten equation competitive inhibition, the Inhibition constant, Ki of the inhibitor is 53.4 μM.

<h3>What is the Ki for the inhibitor?</h3>

The Ki of an inhibitor is known as the inhibition constant.

The inhibition is a competitive inhibition as the Vmax is unchanged but Km changes.

Using the Michaelis-Menten equation for inhibition:

  • Kma = Km/(1 + [I]/Ki)

Making Ki subject of the formula:

  • Ki = [I]/{(Kma/Km) - 1}

where:

  • Kma is the apparent Km due to inhibitor
  • Km is the Km of the enzyme-catalyzed reaction
  • [I] is the concentration of the inhibitor

Solving for Ki:

where

[I] = 26.7 μM

Km = 1.0

Kma = (150% × 1 ) + 1 = 2.5

Ki = 26.7 μM/{(2.5/1) - 1)

Ki = 53.4 μM

Therefore, the Inhibition constant, Ki of the inhibitor is 53.4 μM.

Learn more about enzyme inhibition at: brainly.com/question/13618533

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Answer:

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We have an excess of OH⁻, the ones from the NaOH and the ones that formed the salt NaHCOO, because this salt has this hydrolisis:

NaHCOO  →  Na⁺  +  HCOO⁻

HCOO⁻  +  H₂O  ⇄   HCOOH  +  OH⁻   Kb →  Kw / Ka = 5.55×10⁻¹¹

These contribution of OH⁻ to the solution is insignificant because the Kb is very small

So:  [OH⁻] =  16 mmol / 400 mL →  0.04 M

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