Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Q21:

**Penicillinase and Its Kinetic Properties** Penicillinase, also known as β-lactamase, is a bacterial enzyme that hydrolyzes and inactivates the antibiotic penicillin. Penicillinase follows simple Michaelis–Menten kinetics and reaches half its maximal rate of \(6.8 \times 10^{-10} \, \mu\text{mol} \cdot \text{min}^{-1}\) when the penicillin concentration is \(5.2 \times 10^{-6} \, \text{M}\). **Question:** What would happen to the initial reaction velocity, \(V_0\), of penicillinase if the penicillin concentration were \(10.4 \times 10^{-6} \, \text{M}\)? - \(V_0\) would be greater than \(V_{\max}\). - \(V_0\) would approach \(V_{\max}\). - \(V_0\) would exactly equal \(V_{\max}\). - \(V_0\) would equal half \(V_{\max}\). **Explanation:** This question examines the understanding of the Michaelis-Menten kinetics, specifically focusing on the effect of substrate concentration on enzyme reaction velocity. Given the information that half of \(V_{\max}\) is reached at \(5.2 \times 10^{-6} \, \text{M}\), doubling the substrate concentration to \(10.4 \times 10^{-6} \, \text{M}\) would typically bring the reaction velocity closer to \(V_{\max}\), according to the properties of the Michaelis-Menten curve.
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Transcribed Image Text:**Penicillinase and Its Kinetic Properties** Penicillinase, also known as β-lactamase, is a bacterial enzyme that hydrolyzes and inactivates the antibiotic penicillin. Penicillinase follows simple Michaelis–Menten kinetics and reaches half its maximal rate of \(6.8 \times 10^{-10} \, \mu\text{mol} \cdot \text{min}^{-1}\) when the penicillin concentration is \(5.2 \times 10^{-6} \, \text{M}\). **Question:** What would happen to the initial reaction velocity, \(V_0\), of penicillinase if the penicillin concentration were \(10.4 \times 10^{-6} \, \text{M}\)? - \(V_0\) would be greater than \(V_{\max}\). - \(V_0\) would approach \(V_{\max}\). - \(V_0\) would exactly equal \(V_{\max}\). - \(V_0\) would equal half \(V_{\max}\). **Explanation:** This question examines the understanding of the Michaelis-Menten kinetics, specifically focusing on the effect of substrate concentration on enzyme reaction velocity. Given the information that half of \(V_{\max}\) is reached at \(5.2 \times 10^{-6} \, \text{M}\), doubling the substrate concentration to \(10.4 \times 10^{-6} \, \text{M}\) would typically bring the reaction velocity closer to \(V_{\max}\), according to the properties of the Michaelis-Menten curve.
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